| Year |
Citation |
Score |
| 2021 |
Li J, Han L, Vallese F, Ding Z, Choi SK, Hong S, Luo Y, Liu B, Chan CK, Tajkhorshid E, Zhu J, Clarke O, Zhang K, Gennis R. Cryo-EM structures of cytochrome reveal bound phospholipids and ubiquinone-8 in a dynamic substrate binding site. Proceedings of the National Academy of Sciences of the United States of America. 118. PMID 34417297 DOI: 10.1073/pnas.2106750118 |
0.336 |
|
| 2021 |
Siletsky SA, Soulimane T, Belevich I, Gennis RB, Wikström M. Specific inhibition of proton pumping by the T315V mutation in the K channel of cytochrome ba from Thermus thermophilus. Biochimica Et Biophysica Acta. Bioenergetics. 1862: 148450. PMID 34022199 DOI: 10.1016/j.bbabio.2021.148450 |
0.308 |
|
| 2021 |
Fedotovskaya O, Albertsson I, Nordlund G, Hong S, Gennis RB, Brzezinski P, Ädelroth P. Identification of a cytochrome bc - aa supercomplex in Rhodobacter sphaeroides. Biochimica Et Biophysica Acta. Bioenergetics. 148433. PMID 33932366 DOI: 10.1016/j.bbabio.2021.148433 |
0.533 |
|
| 2021 |
Siletsky SA, Gennis RB. Time-Resolved Electrometric Study of the F→O Transition in Cytochrome c Oxidase. The Effect of Zn Ions on the Positive Side of the Membrane. Biochemistry. Biokhimiia. 86: 105-122. PMID 33705286 DOI: 10.1134/S0006297921010107 |
0.308 |
|
| 2020 |
Iwasaki T, Miyajima-Nakano Y, Fukazawa R, Lin MT, Matsushita SI, Hagiuda E, Taguchi AT, Dikanov SA, Oishi Y, Gennis RB. Escherichia coli amino acid auxotrophic expression host strains for investigating protein structure-function relationships. Journal of Biochemistry. PMID 33289521 DOI: 10.1093/jb/mvaa140 |
0.503 |
|
| 2020 |
Gennis R, Sun C, Benlekbir S, Venkatakrishnan P, Wang Y, Hong S, Hosler J, Tajkhorshid E, Rubinstein JL. Structure of the Alternative Complex III from
Flavobacterium johnsoniae
in a Supercomplex with Cytochrome
c
Oxidase The Faseb Journal. 34: 1-1. DOI: 10.1096/Fasebj.2020.34.S1.00155 |
0.31 |
|
| 2019 |
Xu J, Ding Z, Liu B, Yi SM, Li J, Zhang Z, Liu Y, Li J, Liu L, Zhou A, Gennis RB, Zhu J. Structure of the cytochrome -600 heme-copper menaquinol oxidase bound to inhibitor HQNO shows TM0 is part of the quinol binding site. Proceedings of the National Academy of Sciences of the United States of America. PMID 31888984 DOI: 10.1073/Pnas.1915013117 |
0.615 |
|
| 2019 |
Lencina AM, Gennis RB, Schurig-Briccio LA. The oligomeric state of the Caldivirga maquilingensis type III sulfide:Quinone Oxidoreductase is required for membrane binding. Biochimica Et Biophysica Acta. Bioenergetics. 148132. PMID 31816290 DOI: 10.1016/J.Bbabio.2019.148132 |
0.372 |
|
| 2019 |
Ding Z, Sun C, Yi SM, Gennis RB, Dikanov SA. The ubiquinol binding site of cytochrome from accommodates menaquinone and stabilizes a functional menasemiquinone. Biochemistry. PMID 31644263 DOI: 10.1021/Acs.Biochem.9B00750 |
0.42 |
|
| 2018 |
Melin F, Sabuncu S, Choi SK, Leprince A, Gennis RB, Hellwig P. Role of the tightly bound quinone for the oxygen reaction of cytochrome bo oxidase from E. coli. Febs Letters. PMID 30281793 DOI: 10.1002/1873-3468.13263 |
0.37 |
|
| 2018 |
Ahn YO, Albertsson I, Gennis RB, Ädelroth P. Mechanism of proton transfer through the K proton pathway in the Vibrio cholerae cbb terminal oxidase. Biochimica Et Biophysica Acta. Bioenergetics. 1859: 1191-1198. PMID 30251700 DOI: 10.1016/J.Bbabio.2018.08.002 |
0.451 |
|
| 2018 |
Hards K, McMillan DGG, Schurig-Briccio LA, Gennis RB, Lill H, Bald D, Cook GM. Ionophoric effects of the antitubercular drug bedaquiline. Proceedings of the National Academy of Sciences of the United States of America. PMID 29941569 DOI: 10.1073/Pnas.1803723115 |
0.308 |
|
| 2018 |
Mahinthichaichan P, Gennis RB, Tajkhorshid E. Bacterial denitrifying nitric oxide reductases and aerobic respiratory terminal oxidases use similar delivery pathways for their molecular substrates. Biochimica Et Biophysica Acta. PMID 29883591 DOI: 10.1016/J.Bbabio.2018.06.002 |
0.392 |
|
| 2018 |
Vilhjálmsdóttir J, Gennis RB, Brzezinski P. The electron distribution in the "activated" state of cytochrome c oxidase. Scientific Reports. 8: 7502. PMID 29760451 DOI: 10.1038/S41598-018-25779-W |
0.568 |
|
| 2018 |
Murali R, Gennis RB. Functional importance of Glutamate-445 and Glutamate-99 in proton-coupled electron transfer during oxygen reduction by cytochrome bd from Escherichia coli. Biochimica Et Biophysica Acta. PMID 29719208 DOI: 10.1016/J.Bbabio.2018.04.012 |
0.427 |
|
| 2018 |
Mahinthichaichan P, Gennis RB, Tajkhorshid E. Cytochrome aa3 oxygen reductase utilizes the tunnel observed in the crystal structures to deliver Ofor catalysis. Biochemistry. PMID 29546752 DOI: 10.1021/Acs.Biochem.7B01194 |
0.415 |
|
| 2018 |
Schieferstein JM, Pawate AS, Varel MJ, Guha S, Astrauskaite I, Gennis RB, Kenis PJA. X-ray transparent microfluidic platforms for membrane protein crystallization with microseeds. Lab On a Chip. PMID 29469138 DOI: 10.1039/C7Lc01141E |
0.668 |
|
| 2018 |
Venkatakrishnan P, Benlekbir S, Sun C, Hong S, Hosler J, Rubinstein J, Gennis RB. Characterization of the supercomplex formed by the alternative complex III and the terminal aa3 oxidase from Flavobacterium johnsoniae isolated in styrene:maleic acid copolymer nanodiscs. Biochimica Et Biophysica Acta. PMID 29408430 DOI: 10.1016/J.Bbabio.2018.01.007 |
0.347 |
|
| 2018 |
Graf S, Hong S, Gennis R, von Ballmoos C. Resolving the mechanism of proton pumping coupled to hydride transfer in E. coli Transhydrogenase Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 1859: e119. DOI: 10.1016/J.Bbabio.2018.09.352 |
0.356 |
|
| 2017 |
Taguchi AT, Miyajima-Nakano Y, Fukazawa R, Lin MT, Baldansuren A, Gennis RB, Hasegawa K, Kumasaka T, Dikanov SA, Iwasaki T. Unpaired Electron Spin Density Distribution across Reduced [2Fe-2S] Cluster Ligands by 13Cβ-Cysteine Labeling. Inorganic Chemistry. PMID 29278328 DOI: 10.1021/Acs.Inorgchem.7B02676 |
0.544 |
|
| 2017 |
Galván AE, Chalón MC, Schurig-Briccio LA, Salomón RA, Minahk CJ, Gennis RB, Bellomio A. Cytochromes bd-I and bo are essential for the bactericidal effect of microcin J25 on Escherichia coli cells. Biochimica Et Biophysica Acta. Bioenergetics. 1859: 110-118. PMID 29107655 DOI: 10.1016/J.Bbabio.2017.10.006 |
0.356 |
|
| 2017 |
Padayatti PS, Leung JH, Mahinthichaichan P, Tajkhorshid E, Ishchenko A, Cherezov V, Soltis SM, Jackson JB, Stout CD, Gennis RB, Zhang Q. Critical Role of Water Molecules in Proton Translocation by the Membrane-Bound Transhydrogenase. Structure (London, England : 1993). PMID 28648609 DOI: 10.1016/J.Str.2017.05.022 |
0.406 |
|
| 2017 |
Choi SK, Schurig-Briccio L, Ding Z, Hong S, Sun C, Gennis RB. Location of the substrate binding site of the cytochrome bo3 ubiquinol oxidase from Escherichia coli. Journal of the American Chemical Society. PMID 28538096 DOI: 10.1021/Jacs.7B03883 |
0.398 |
|
| 2017 |
Schieferstein JM, Pawate AS, Sun C, Wan F, Sheraden PN, Broecker J, Ernst OP, Gennis RB, Kenis PJA. X-ray transparent microfluidic chips for high-throughput screening and optimization of in meso membrane protein crystallization. Biomicrofluidics. 11: 024118. PMID 28469762 DOI: 10.1063/1.4981818 |
0.693 |
|
| 2017 |
Choi SK, Lin MT, Ouyang H, Gennis RB. Searching for the low affinity ubiquinone binding site in cytochrome bo3 from Escherichia coli. Biochimica Et Biophysica Acta. PMID 28235459 DOI: 10.1016/J.Bbabio.2017.02.008 |
0.606 |
|
| 2017 |
von Ballmoos C, Smirnova I, Poiana F, Gonska N, Chang H, Gennis RB, Brzezinski P, Ädelroth P. Dynamics of the KBProton Pathway in Cytochromeba3fromThermus thermophilus Israel Journal of Chemistry. 57: 424-436. DOI: 10.1002/Ijch.201600136 |
0.729 |
|
| 2016 |
Melin F, Xie H, Meyer T, Ahn YO, Gennis RB, Michel H, Hellwig P. The unusual redox properties of C-type oxidases. Biochimica Et Biophysica Acta. PMID 27664317 DOI: 10.1016/J.Bbabio.2016.09.009 |
0.439 |
|
| 2016 |
Sun C, Taguchi AT, Vermaas JV, Beal NJ, O'Malley PJ, Tajkhorshid E, Gennis RB, Dikanov SA. Q-band ENDOR reveals out of plane hydrogen bonds stabilize an anionic ubisemiquinone in cytochrome bo3 from Escherichia coli. Biochemistry. PMID 27622672 DOI: 10.1021/Acs.Biochem.6B00669 |
0.356 |
|
| 2016 |
Hammer ND, Schurig-Briccio LA, Gerdes SY, Gennis RB, Skaar EP. CtaM Is Required for Menaquinol Oxidase aa3 Function in Staphylococcus aureus. Mbio. 7. PMID 27406563 DOI: 10.1128/Mbio.00823-16 |
0.335 |
|
| 2016 |
Gennis RB. Proton Dynamics at the Membrane Surface. Biophysical Journal. 110: 1909-11. PMID 27166799 DOI: 10.1016/J.Bpj.2016.04.001 |
0.362 |
|
| 2016 |
Hosseinzadeh P, Tian S, Marshall NM, Hemp J, Mullen T, Nilges MJ, Gao YG, Robinson H, Stahl DA, Gennis RB, Lu Y. A Purple Cupredoxin from Nitrosopumilus maritimus Containing a Mononuclear Type 1 Copper Center with an Open Binding Site. Journal of the American Chemical Society. PMID 27120678 DOI: 10.1021/Jacs.5B13128 |
0.335 |
|
| 2016 |
Cassano JA, Choi SK, McDonald W, Szundi I, Villa Gawboy TR, Gennis RB, Einarsdóttir Ó. The CO Photodissociation and Recombination Dynamics of the W172Y/F282T Ligand Channel Mutant of Rhodobacter sphaeroides aa3 Cytochrome c Oxidase. Photochemistry and Photobiology. PMID 27029379 DOI: 10.1111/Php.12587 |
0.412 |
|
| 2016 |
Mahinthichaichan P, Gennis RB, Tajkhorshid E. All the O2 consumed by Thermus thermophilus cytochrome ba3 is delivered to the active site through a long, open hydrophobic tunnel with entrances within the lipid bilayer. Biochemistry. PMID 26845082 DOI: 10.1021/Acs.Biochem.5B01255 |
0.38 |
|
| 2016 |
Mahinthichaichan P, Gennis RB, Tajkhorshid E. Characterizations of Substrate Delivery Pathways in the Nitric Oxide Reductase Biophysical Journal. 110: 314a. DOI: 10.1016/J.Bpj.2015.11.1685 |
0.406 |
|
| 2015 |
Hong S, de Almeida WB, Taguchi AT, Samoilova RI, Gennis RB, O'Malley PJ, Dikanov SA, Crofts AR. Correction to The Semiquinone at the Qi Site of the bc1 Complex Explored Using HYSCORE Spectroscopy and Specific Isotopic Labeling of Ubiquinone in Rhodobacter sphaeroides via (13)C Methionine and Construction of a Methionine Auxotroph. Biochemistry. PMID 26623932 DOI: 10.1021/Acs.Biochem.5B01251 |
0.324 |
|
| 2015 |
Lin MT, Fukazawa R, Miyajima-Nakano Y, Matsushita S, Choi SK, Iwasaki T, Gennis RB. Escherichia coli Auxotroph Host Strains for Amino Acid-Selective Isotope Labeling of Recombinant Proteins. Methods in Enzymology. 565: 45-66. PMID 26577727 DOI: 10.1016/Bs.Mie.2015.05.012 |
0.557 |
|
| 2015 |
Yi SM, Taguchi AT, Samoilova RI, O'Malley PJ, Gennis RB, Dikanov SA. Plasticity in the High Affinity Menaquinone Binding Site of the Cytochrome aa3-600 Menaquinol Oxidase from Bacillus subtilis. Biochemistry. 54: 5030-44. PMID 26196462 DOI: 10.1021/Acs.Biochem.5B00528 |
0.472 |
|
| 2015 |
Jackson JB, Leung JH, Stout CD, Schurig-Briccio LA, Gennis RB. Review and Hypothesis. New insights into the reaction mechanism of transhydrogenase: Swivelling the dIII component may gate the proton channel. Febs Letters. 589: 2027-33. PMID 26143375 DOI: 10.1016/J.Febslet.2015.06.027 |
0.396 |
|
| 2015 |
Ahn YO, Lee HJ, Kaluka D, Yeh SR, Rousseau DL, Ädelroth P, Gennis RB. The two transmembrane helices of CcoP are sufficient for assembly of the cbb3-type heme-copper oxygen reductase from Vibrio cholerae. Biochimica Et Biophysica Acta. PMID 26116881 DOI: 10.1016/J.Bbabio.2015.06.013 |
0.461 |
|
| 2015 |
von Ballmoos C, Gonska N, Lachmann P, Gennis RB, Ädelroth P, Brzezinski P. Mutation of a single residue in the ba3 oxidase specifically impairs protonation of the pump site. Proceedings of the National Academy of Sciences of the United States of America. 112: 3397-402. PMID 25733886 DOI: 10.1073/Pnas.1422434112 |
0.653 |
|
| 2015 |
Leung JH, Schurig-Briccio LA, Yamaguchi M, Moeller A, Speir JA, Gennis RB, Stout CD. Structural biology. Division of labor in transhydrogenase by alternating proton translocation and hydride transfer. Science (New York, N.Y.). 347: 178-81. PMID 25574024 DOI: 10.1126/Science.1260451 |
0.384 |
|
| 2015 |
Lin MT, Fukazawa R, Miyajima-Nakano Y, Matsushita S, Choi SK, Iwasaki T, Gennis RB. Escherichia coli Auxotroph Host Strains for Amino Acid-Selective Isotope Labeling of Recombinant Proteins Methods in Enzymology. DOI: 10.1016/bs.mie.2015.05.012 |
0.48 |
|
| 2014 |
Ahn YO, Mahinthichaichan P, Lee HJ, Ouyang H, Kaluka D, Yeh SR, Arjona D, Rousseau DL, Tajkhorshid E, Adelroth P, Gennis RB. Conformational coupling between the active site and residues within the K(C)-channel of the Vibrio cholerae cbb3-type (C-family) oxygen reductase. Proceedings of the National Academy of Sciences of the United States of America. 111: E4419-28. PMID 25288772 DOI: 10.1073/Pnas.1411676111 |
0.428 |
|
| 2014 |
Hong S, de Almeida WB, Taguchi AT, Samoilova RI, Gennis RB, O'Malley PJ, Dikanov SA, Crofts AR. The semiquinone at the Qi site of the bc1 complex explored using HYSCORE spectroscopy and specific isotopic labeling of ubiquinone in Rhodobacter sphaeroides via (13)C methionine and construction of a methionine auxotroph. Biochemistry. 53: 6022-31. PMID 25184535 DOI: 10.1021/Bi500654Y |
0.349 |
|
| 2014 |
Szundi I, Kittredge C, Choi SK, McDonald W, Ray J, Gennis RB, Einarsdóttir Ó. Kinetics and intermediates of the reaction of fully reduced Escherichia coli bo₃ ubiquinol oxidase with O₂. Biochemistry. 53: 5393-404. PMID 25076393 DOI: 10.1021/Bi500567M |
0.356 |
|
| 2014 |
Meyer T, Melin F, Xie H, von der Hocht I, Choi SK, Noor MR, Michel H, Gennis RB, Soulimane T, Hellwig P. Evidence for distinct electron transfer processes in terminal oxidases from different origin by means of protein film voltammetry. Journal of the American Chemical Society. 136: 10854-7. PMID 25054669 DOI: 10.1021/Ja505126V |
0.368 |
|
| 2014 |
Svahn E, Faxén K, Gennis RB, Brzezinski P. Proton pumping by an inactive structural variant of cytochrome c oxidase. Journal of Inorganic Biochemistry. 140: 6-11. PMID 25042731 DOI: 10.1016/J.Jinorgbio.2014.06.016 |
0.614 |
|
| 2014 |
Bricio C, Alvarez L, San Martin M, Schurig-Briccio LA, Gennis RB, Berenguer J. A third subunit in ancestral cytochrome c-dependent nitric oxide reductases. Applied and Environmental Microbiology. 80: 4871-8. PMID 24907324 DOI: 10.1128/Aem.00790-14 |
0.338 |
|
| 2014 |
Schurig-Briccio LA, Yano T, Rubin H, Gennis RB. Characterization of the type 2 NADH:menaquinone oxidoreductases from Staphylococcus aureus and the bactericidal action of phenothiazines. Biochimica Et Biophysica Acta. 1837: 954-63. PMID 24709059 DOI: 10.1016/J.Bbabio.2014.03.017 |
0.306 |
|
| 2014 |
Hoeser J, Hong S, Gehmann G, Gennis RB, Friedrich T. Subunit CydX of Escherichia coli cytochrome bd ubiquinol oxidase is essential for assembly and stability of the di-heme active site. Febs Letters. 588: 1537-41. PMID 24681096 DOI: 10.1016/J.Febslet.2014.03.036 |
0.423 |
|
| 2014 |
Y?ld?z GG, Gennis RB, Daldal F, Öztürk M. The K(C) channel in the cbb3-type respiratory oxygen reductase from Rhodobacter capsulatus is required for both chemical and pumped protons. Journal of Bacteriology. 196: 1825-32. PMID 24563037 DOI: 10.1128/Jb.00005-14 |
0.441 |
|
| 2014 |
Leung J, Schurig-Briccio L, Yamaguchi M, Moeller A, Speir J, Gennis R, Stout C. Transhydrogenase coupling proton translocation and hydride transfer Acta Crystallographica Section a Foundations and Advances. 70: C1495-C1495. DOI: 10.1107/S2053273314085040 |
0.31 |
|
| 2014 |
Cassano JA, Choi S, Gawboy TV, Gennis RB, Einarsdóttir O. Spectroscopic Investigation of the Roles of F282 and W172 in the Ligand Pathway of Aa3 Cytochrome C Oxidase from Rhodobacter Sphaeroides Biophysical Journal. 106: 587a. DOI: 10.1016/J.Bpj.2013.11.3254 |
0.415 |
|
| 2014 |
Hoeser J, Gehmann G, Gennis RB, Friedrich T. CydX is a subunit of Escherichia coli cytochrome bd terminal oxidase and essential for assembly and stability of the di-heme active site Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 1837: e98-e99. DOI: 10.1016/J.Bbabio.2014.05.173 |
0.356 |
|
| 2014 |
Brzezinski P, von Ballmoos C, Ädelroth P, Gennis RB, Smirnova I, Vilhjálmsdóttir J. Choreography and architecture of the proton-pumping machinery in respiratory oxidases Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 1837: e5. DOI: 10.1016/J.Bbabio.2014.05.124 |
0.564 |
|
| 2013 |
Smirnova I, Chang HY, von Ballmoos C, Ädelroth P, Gennis RB, Brzezinski P. Single mutations that redirect internal proton transfer in the ba3 oxidase from Thermus thermophilus. Biochemistry. 52: 7022-30. PMID 24004023 DOI: 10.1021/Bi4008726 |
0.739 |
|
| 2013 |
Schurig-Briccio LA, Venkatakrishnan P, Hemp J, Bricio C, Berenguer J, Gennis RB. Characterization of the nitric oxide reductase from Thermus thermophilus. Proceedings of the National Academy of Sciences of the United States of America. 110: 12613-8. PMID 23858452 DOI: 10.1073/Pnas.1301731110 |
0.396 |
|
| 2013 |
Johansson AL, Högbom M, Carlsson J, Gennis RB, Brzezinski P. Role of aspartate 132 at the orifice of a proton pathway in cytochrome c oxidase. Proceedings of the National Academy of Sciences of the United States of America. 110: 8912-7. PMID 23674679 DOI: 10.1073/Pnas.1303954110 |
0.637 |
|
| 2013 |
Sperling LJ, Tang M, Berthold DA, Nesbitt AE, Gennis RB, Rienstra CM. Solid-state NMR study of a 41 kDa membrane protein complex DsbA/DsbB. The Journal of Physical Chemistry. B. 117: 6052-60. PMID 23527473 DOI: 10.1021/Jp400795D |
0.412 |
|
| 2013 |
Tang M, Nesbitt AE, Sperling LJ, Berthold DA, Schwieters CD, Gennis RB, Rienstra CM. Structure of the disulfide bond generating membrane protein DsbB in the lipid bilayer. Journal of Molecular Biology. 425: 1670-82. PMID 23416557 DOI: 10.1016/J.Jmb.2013.02.009 |
0.337 |
|
| 2013 |
Venkatakrishnan P, Lencina AM, Schurig-Briccio LA, Gennis RB. Alternate pathways for NADH oxidation in Thermus thermophilus using type 2 NADH dehydrogenases. Biological Chemistry. 394: 667-76. PMID 23370906 DOI: 10.1515/Hsz-2012-0333 |
0.389 |
|
| 2013 |
Johansson AL, Carlsson J, Högbom M, Hosler JP, Gennis RB, Brzezinski P. Proton uptake and pKa changes in the uncoupled Asn139Cys variant of cytochrome c oxidase. Biochemistry. 52: 827-36. PMID 23305515 DOI: 10.1021/Bi301597A |
0.65 |
|
| 2013 |
Lencina AM, Ding Z, Schurig-Briccio LA, Gennis RB. Characterization of the Type III sulfide:quinone oxidoreductase from Caldivirga maquilingensis and its membrane binding. Biochimica Et Biophysica Acta. 1827: 266-75. PMID 23103448 DOI: 10.1016/J.Bbabio.2012.10.010 |
0.449 |
|
| 2013 |
Mahinthichaichan P, Gennis RB, Tajkhorshid E. Comparative Investigation of O2 Delivery Pathwys in A-Type and B-Type Cytochrome C Oxidases Biophysical Journal. 104: 487a. DOI: 10.1016/J.Bpj.2012.11.2686 |
0.424 |
|
| 2012 |
Iwasaki T, Fukazawa R, Miyajima-Nakano Y, Baldansuren A, Matsushita S, Lin MT, Gennis RB, Hasegawa K, Kumasaka T, Dikanov SA. Dissection of hydrogen bond interaction network around an iron-sulfur cluster by site-specific isotope labeling of hyperthermophilic archaeal Rieske-type ferredoxin. Journal of the American Chemical Society. 134: 19731-8. PMID 23145461 DOI: 10.1021/Ja308049U |
0.523 |
|
| 2012 |
Szundi I, Funatogawa C, Cassano J, McDonald W, Ray J, Hiser C, Ferguson-Miller S, Gennis RB, Einarsdóttir Ó. Spectral identification of intermediates generated during the reaction of dioxygen with the wild-type and EQ(I-286) mutant of Rhodobacter sphaeroides cytochrome c oxidase. Biochemistry. 51: 9302-11. PMID 23057757 DOI: 10.1021/Bi301166U |
0.438 |
|
| 2012 |
Morgan JE, Vakkasoglu AS, Lanyi JK, Lugtenburg J, Gennis RB, Maeda A. Structure changes upon deprotonation of the proton release group in the bacteriorhodopsin photocycle. Biophysical Journal. 103: 444-52. PMID 22947860 DOI: 10.1016/J.Bpj.2012.06.022 |
0.782 |
|
| 2012 |
Ouyang H, Han H, Roh JH, Hemp J, Hosler JP, Gennis RB. Functional importance of a pair of conserved glutamic acid residues and of Ca(2+) binding in the cbb(3)-type oxygen reductases from Rhodobacter sphaeroides and Vibrio cholerae. Biochemistry. 51: 7290-6. PMID 22913716 DOI: 10.1021/Bi3006847 |
0.616 |
|
| 2012 |
Murali R, Yildiz GG, Daldal F, Gennis RB. Stoichiometry of proton pumping by the cbb3-type oxygen reductase in whole cells of Rhodobacter capsulatus at pH 7 is about 0.5 H+ per electron. Proceedings of the National Academy of Sciences of the United States of America. 109: E2144; author reply . PMID 22761318 DOI: 10.1073/Pnas.1207216109 |
0.395 |
|
| 2012 |
von Ballmoos C, Lachmann P, Gennis RB, Ädelroth P, Brzezinski P. Timing of electron and proton transfer in the ba(3) cytochrome c oxidase from Thermus thermophilus. Biochemistry. 51: 4507-17. PMID 22624600 DOI: 10.1021/Bi300132T |
0.637 |
|
| 2012 |
Lin MT, Gennis RB. Product-controlled steady-state kinetics between cytochrome aa(3) from Rhodobacter sphaeroides and equine ferrocytochrome c analyzed by a novel spectrophotometric approach. Biochimica Et Biophysica Acta. 1817: 1894-900. PMID 22516686 DOI: 10.1016/J.Bbabio.2012.04.001 |
0.597 |
|
| 2012 |
Lin MT, Baldansuren A, Hart R, Samoilova RI, Narasimhulu KV, Yap LL, Choi SK, O'Malley PJ, Gennis RB, Dikanov SA. Interactions of intermediate semiquinone with surrounding protein residues at the Q(H) site of wild-type and D75H mutant cytochrome bo3 from Escherichia coli. Biochemistry. 51: 3827-38. PMID 22497216 DOI: 10.1021/Bi300151Q |
0.769 |
|
| 2012 |
Chang HY, Choi SK, Vakkasoglu AS, Chen Y, Hemp J, Fee JA, Gennis RB. Exploring the proton pump and exit pathway for pumped protons in cytochrome ba3 from Thermus thermophilus. Proceedings of the National Academy of Sciences of the United States of America. 109: 5259-64. PMID 22431640 DOI: 10.1073/Pnas.1107345109 |
0.813 |
|
| 2012 |
Näsvik Öjemyr L, von Ballmoos C, Gennis RB, Sligar SG, Brzezinski P. Reconstitution of respiratory oxidases in membrane nanodiscs for investigation of proton-coupled electron transfer. Febs Letters. 586: 640-5. PMID 22209982 DOI: 10.1016/J.Febslet.2011.12.023 |
0.571 |
|
| 2012 |
von Ballmoos C, Adelroth P, Gennis RB, Brzezinski P. Proton transfer in ba(3) cytochrome c oxidase from Thermus thermophilus. Biochimica Et Biophysica Acta. 1817: 650-7. PMID 22172736 DOI: 10.1016/J.Bbabio.2011.11.015 |
0.644 |
|
| 2012 |
Iwamoto Y, Ando Y, Muramoto K, Gennis R, Shiro Y. 2PT155 Oxygen consumption activity of cbb_3-type cytochrome c oxidase(The 50th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 52: S131. DOI: 10.2142/Biophys.52.S131_4 |
0.3 |
|
| 2012 |
Han H, Hemp J, Pace LA, Ouyang H, Ganesan K, Roh JH, Daldal F, Blanke SR, Gennis RB. Adaptation of aerobic respiration to low O2 environments (Proceedings of the National Academy of Sciences of the United States of America (2011) 108, 34, (14109-14114) DOI: 10.1073/pnas.1018958108) Proceedings of the National Academy of Sciences of the United States of America. 109: 7947. DOI: 10.1073/Pnas.1205903109 |
0.64 |
|
| 2012 |
Mahinthichaichan P, Hemp J, Gennis RB, Tajkhorshid E. Probing Gas Diffusion Pathways in Cytochrome C Oxidase with Explicit and Implicit Ligand Samplings Biophysical Journal. 102: 713a. DOI: 10.1016/J.Bpj.2011.11.3870 |
0.386 |
|
| 2012 |
Naumann RL, Nowak C, Schwaighofer A, Ferguson-Miller S, Gennis RB, Knoll W. Protein Dynamics Coupled to Electron Transfer in Cytochrome C Oxidase from R. Sphaeroides by Time-Resolved Surface-Enhanced 2D-IR-Absorption Spectroscopy Biophysical Journal. 102: 50a. DOI: 10.1016/J.Bpj.2011.11.303 |
0.385 |
|
| 2012 |
Chang H, Choi S, Vakkasoglu A, Chen Y, Hemp J, Fee J, Gennis R. Investigation of the proton pump and exit pathway in cytochrome ba3 from Thermus thermophilus Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 1817: S106. DOI: 10.1016/J.Bbabio.2012.06.286 |
0.798 |
|
| 2012 |
Bloch DA, Borisov VB, Murali R, Verkhovskaya ML, Han H, Gennis RB, Verkhovsky MI. Cytochrome bd-II from aerobic respiratory chain of Escherichia coli is a proton-motive force generator Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 1817: S105. DOI: 10.1016/J.Bbabio.2012.06.283 |
0.573 |
|
| 2012 |
Ahn Y, Gennis RB. The electron transfer pathway of Type-C oxygen reductase from V. cholera Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 1817: S104. DOI: 10.1016/J.Bbabio.2012.06.280 |
0.347 |
|
| 2011 |
Lee HJ, Gennis RB, Ädelroth P. Entrance of the proton pathway in cbb3-type heme-copper oxidases. Proceedings of the National Academy of Sciences of the United States of America. 108: 17661-6. PMID 21997215 DOI: 10.1073/Pnas.1107543108 |
0.439 |
|
| 2011 |
Borisov VB, Murali R, Verkhovskaya ML, Bloch DA, Han H, Gennis RB, Verkhovsky MI. Aerobic respiratory chain of Escherichia coli is not allowed to work in fully uncoupled mode. Proceedings of the National Academy of Sciences of the United States of America. 108: 17320-4. PMID 21987791 DOI: 10.1073/Pnas.1108217108 |
0.614 |
|
| 2011 |
Lin MT, Sperling LJ, Frericks Schmidt HL, Tang M, Samoilova RI, Kumasaka T, Iwasaki T, Dikanov SA, Rienstra CM, Gennis RB. A rapid and robust method for selective isotope labeling of proteins. Methods (San Diego, Calif.). 55: 370-8. PMID 21925267 DOI: 10.1016/J.Ymeth.2011.08.019 |
0.572 |
|
| 2011 |
Han H, Hemp J, Pace LA, Ouyang H, Ganesan K, Roh JH, Daldal F, Blanke SR, Gennis RB. Adaptation of aerobic respiration to low O2 environments. Proceedings of the National Academy of Sciences of the United States of America. 108: 14109-14. PMID 21844375 DOI: 10.1073/Pnas.1018958108 |
0.698 |
|
| 2011 |
Borisov VB, Gennis RB, Hemp J, Verkhovsky MI. The cytochrome bd respiratory oxygen reductases. Biochimica Et Biophysica Acta. 1807: 1398-413. PMID 21756872 DOI: 10.1016/J.Bbabio.2011.06.016 |
0.445 |
|
| 2011 |
von Ballmoos C, Gennis RB, Ädelroth P, Brzezinski P. Kinetic design of the respiratory oxidases. Proceedings of the National Academy of Sciences of the United States of America. 108: 11057-62. PMID 21690359 DOI: 10.1073/Pnas.1104103108 |
0.626 |
|
| 2011 |
Egawa T, Ganesan K, Lin MT, Yu MA, Hosler JP, Yeh SR, Rousseau DL, Gennis RB. Differential effects of glutamate-286 mutations in the aa(3)-type cytochrome c oxidase from Rhodobacter sphaeroides and the cytochrome bo(3) ubiquinol oxidase from Escherichia coli. Biochimica Et Biophysica Acta. 1807: 1342-8. PMID 21684251 DOI: 10.1016/J.Bbabio.2011.06.001 |
0.74 |
|
| 2011 |
Nowak C, Laredo T, Gebert J, Lipkowski J, Gennis RB, Ferguson-Miller S, Knoll W, Naumann RL. 2D-SEIRA spectroscopy to highlight conformational changes of the cytochrome c oxidase induced by direct electron transfer. Metallomics : Integrated Biometal Science. 3: 619-27. PMID 21541411 DOI: 10.1039/C0Mt00083C |
0.407 |
|
| 2011 |
Tang M, Sperling LJ, Berthold DA, Nesbitt AE, Gennis RB, Rienstra CM. Solid-state NMR study of the charge-transfer complex between ubiquinone-8 and disulfide bond generating membrane protein DsbB. Journal of the American Chemical Society. 133: 4359-66. PMID 21375236 DOI: 10.1021/Ja107775W |
0.412 |
|
| 2011 |
Lin MT, Shubin AA, Samoilova RI, Narasimhulu KV, Baldansuren A, Gennis RB, Dikanov SA. Exploring by pulsed EPR the electronic structure of ubisemiquinone bound at the QH site of cytochrome bo3 from Escherichia coli with in vivo 13C-labeled methyl and methoxy substituents. The Journal of Biological Chemistry. 286: 10105-14. PMID 21247900 DOI: 10.1074/Jbc.M110.206821 |
0.639 |
|
| 2011 |
Maeda A, Morgan JE, Vakkasoglu AS, Lanyi JK, Lugtenburg J, Gennis RB. 2Q1436 Structural Rearrangement for the Unidirectional Proton Transfer in the Bacteriorhodopsin Photocycle : A Time-resolved FTIR Study(Photobiology: Vision & Photoreception 2,The 48th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 51: S102. DOI: 10.2142/Biophys.51.S102_1 |
0.756 |
|
| 2011 |
Naumann RC, Nowak C, Walz D, Gennis RB, Ferguson-Miller S, Knoll W. Kinetics of the Cytochrome C Oxidase from R. Sphaeroidis Under Turn-Over Conditions by Time-Resolved Surface-Enhanced Infrared Absorption Spectroscopy (SEIRas) Biophysical Journal. 100: 547a. DOI: 10.1016/J.Bpj.2010.12.3190 |
0.433 |
|
| 2011 |
Nowak C, Schach D, Gebert J, Grosserueschkamp M, Gennis RB, Ferguson-Miller S, Knoll W, Walz D, Naumann RLC. Oriented immobilization and electron transfer to the cytochrome c oxidase Journal of Solid State Electrochemistry. 15: 105-114. DOI: 10.1007/S10008-010-1032-X |
0.351 |
|
| 2010 |
Bolshakov IA, Vygodina TV, Gennis R, Karyakin AA, Konstantinov AA. Catalase activity of cytochrome c oxidase assayed with hydrogen peroxide-sensitive electrode microsensor Biochemistry (Moscow). 75: 1352-1360. PMID 21314602 DOI: 10.1134/S0006297910110064 |
0.41 |
|
| 2010 |
Lee HJ, Svahn E, Swanson JM, Lepp H, Voth GA, Brzezinski P, Gennis RB. Intricate role of water in proton transport through cytochrome c oxidase. Journal of the American Chemical Society. 132: 16225-39. PMID 20964330 DOI: 10.1021/Ja107244G |
0.655 |
|
| 2010 |
Ojemyr LN, Lee HJ, Gennis RB, Brzezinski P. Functional interactions between membrane-bound transporters and membranes. Proceedings of the National Academy of Sciences of the United States of America. 107: 15763-7. PMID 20798065 DOI: 10.1073/Pnas.1006109107 |
0.575 |
|
| 2010 |
Chang HY, Ahn Y, Pace LA, Lin MT, Lin YH, Gennis RB. The diheme cytochrome c(4) from Vibrio cholerae is a natural electron donor to the respiratory cbb(3) oxygen reductase. Biochemistry. 49: 7494-503. PMID 20715760 DOI: 10.1021/Bi1004574 |
0.716 |
|
| 2010 |
Smirnova I, Reimann J, von Ballmoos C, Chang HY, Gennis RB, Fee JA, Brzezinski P, Adelroth P. Functional role of Thr-312 and Thr-315 in the proton-transfer pathway in ba3 Cytochrome c oxidase from Thermus thermophilus. Biochemistry. 49: 7033-9. PMID 20677778 DOI: 10.1021/Bi100749P |
0.713 |
|
| 2010 |
Oganesyan VS, White GF, Field S, Marritt S, Gennis RB, Yap LL, Thomson AJ. Nitroxide spin labels as EPR reporters of the relaxation and magnetic properties of the heme-copper site in cytochrome bo3, E. coli. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 15: 1255-64. PMID 20623242 DOI: 10.1007/S00775-010-0683-5 |
0.715 |
|
| 2010 |
Rappaport F, Zhang J, Vos MH, Gennis RB, Borisov VB. Heme-heme and heme-ligand interactions in the di-heme oxygen-reducing site of cytochrome bd from Escherichia coli revealed by nanosecond absorption spectroscopy. Biochimica Et Biophysica Acta. 1797: 1657-64. PMID 20529691 DOI: 10.1016/J.Bbabio.2010.05.010 |
0.413 |
|
| 2010 |
Zhu J, Han H, Pawate A, Gennis RB. Decoupling mutations in the D-channel of the aa(3)-type cytochrome c oxidase from Rhodobacter sphaeroides suggest that a continuous hydrogen-bonded chain of waters is essential for proton pumping. Biochemistry. 49: 4476-82. PMID 20441187 DOI: 10.1021/Bi100344X |
0.823 |
|
| 2010 |
Yap LL, Lin MT, Ouyang H, Samoilova RI, Dikanov SA, Gennis RB. The quinone-binding sites of the cytochrome bo3 ubiquinol oxidase from Escherichia coli. Biochimica Et Biophysica Acta. 1797: 1924-32. PMID 20416270 DOI: 10.1016/J.Bbabio.2010.04.011 |
0.788 |
|
| 2010 |
Yi SM, Narasimhulu KV, Samoilova RI, Gennis RB, Dikanov SA. Characterization of the semiquinone radical stabilized by the cytochrome aa3-600 menaquinol oxidase of Bacillus subtilis. The Journal of Biological Chemistry. 285: 18241-51. PMID 20351111 DOI: 10.1074/jbc.M110.116186 |
0.341 |
|
| 2010 |
Ganesan K, Gennis RB. Blocking the K-pathway still allows rapid one-electron reduction of the binuclear center during the anaerobic reduction of the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides. Biochimica Et Biophysica Acta. 1797: 619-24. PMID 20307488 DOI: 10.1016/J.Bbabio.2010.03.012 |
0.593 |
|
| 2010 |
Morgan JE, Vakkasoglu AS, Lanyi JK, Gennis RB, Maeda A. Coordinating the structural rearrangements associated with unidirectional proton transfer in the bacteriorhodopsin photocycle induced by deprotonation of the proton-release group: a time-resolved difference FTIR spectroscopic study. Biochemistry. 49: 3273-81. PMID 20232848 DOI: 10.1021/Bi901757Y |
0.783 |
|
| 2010 |
Siletsky SA, Zhu J, Gennis RB, Konstantinov AA. Partial steps of charge translocation in the nonpumping N139L mutant of Rhodobacter sphaeroides cytochrome c oxidase with a blocked D-channel. Biochemistry. 49: 3060-73. PMID 20192226 DOI: 10.1021/Bi901719E |
0.609 |
|
| 2010 |
Namslauer I, Lee HJ, Gennis RB, Brzezinski P. A pathogenic mutation in cytochrome c oxidase results in impaired proton pumping while retaining O(2)-reduction activity. Biochimica Et Biophysica Acta. 1797: 550-6. PMID 20117076 DOI: 10.1016/J.Bbabio.2010.01.027 |
0.643 |
|
| 2010 |
Nowak C, Santonicola MG, Schach D, Zhu J, Gennis RB, Ferguson-Miller S, Baurecht D, Walz D, Knoll W, Naumann RLC. Conformational transitions and molecular hysteresis of cytochrome c oxidase: Varying the redox state by electronic wiring Soft Matter. 6: 5523-5532. DOI: 10.1039/C0Sm00160K |
0.611 |
|
| 2010 |
Schach D, Nowak C, Gennis RB, Ferguson-Miller S, Knoll W, Walz D, Naumann RLC. Modeling direct electron transfer to a multi-redox center protein: Cytochrome c Oxidase Journal of Electroanalytical Chemistry. 649: 268-276. DOI: 10.1016/J.Jelechem.2010.07.009 |
0.384 |
|
| 2010 |
Naumann RL, Nowak C, Walz D, Gennis RB. How Electron Transfer Is Linked to Conformational Transitions of Peptide Groups of the Cytochrome C Oxidase, a Study By 2d-Ir Spectro-Electrochemistry Biophysical Journal. 98: 24a. DOI: 10.1016/J.Bpj.2009.12.142 |
0.368 |
|
| 2010 |
Nowak C, Knoll W, Walz D, Gennis RB, Naumann RL. Conformational Transitions Associated with Electrochemically-Induced Redox Processes Through the Cytochrome C Oxidase Followed by Time-Resolved 2d-Surface-Enhanced Infrared Absorption Spectroscopy (tr-2d-Seiras) Biophysical Journal. 98: 23a-24a. DOI: 10.1016/J.Bpj.2009.12.140 |
0.374 |
|
| 2009 |
Egawa T, Lin MT, Hosler JP, Gennis RB, Yeh SR, Rousseau DL. Communication between R481 and Cu(B) in cytochrome bo(3) ubiquinol oxidase from Escherichia coli. Biochemistry. 48: 12113-24. PMID 19928831 DOI: 10.1021/Bi901187U |
0.651 |
|
| 2009 |
Chang HY, Hemp J, Chen Y, Fee JA, Gennis RB. The cytochrome ba3 oxygen reductase from Thermus thermophilus uses a single input channel for proton delivery to the active site and for proton pumping. Proceedings of the National Academy of Sciences of the United States of America. 106: 16169-73. PMID 19805275 DOI: 10.1073/Pnas.0905264106 |
0.66 |
|
| 2009 |
Lee HJ, Ojemyr L, Vakkasoglu A, Brzezinski P, Gennis RB. Properties of Arg481 mutants of the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides suggest that neither R481 nor the nearby D-propionate of heme a3 is likely to be the proton loading site of the proton pump. Biochemistry. 48: 7123-31. PMID 19575527 DOI: 10.1021/Bi901015D |
0.839 |
|
| 2009 |
Egawa T, Lee HJ, Ji H, Gennis RB, Yeh SR, Rousseau DL. Identification of heme propionate vibrational modes in the resonance Raman spectra of cytochrome c oxidase. Analytical Biochemistry. 394: 141-3. PMID 19563766 DOI: 10.1016/J.Ab.2009.06.035 |
0.365 |
|
| 2009 |
Egawa T, Lee HJ, Gennis RB, Yeh SR, Rousseau DL. Critical structural role of R481 in cytochrome c oxidase from Rhodobacter sphaeroides. Biochimica Et Biophysica Acta. 1787: 1272-5. PMID 19463779 DOI: 10.1016/J.Bbabio.2009.05.006 |
0.398 |
|
| 2009 |
Hayashi T, Lin MT, Ganesan K, Chen Y, Fee JA, Gennis RB, Moënne-Loccoz P. Accommodation of two diatomic molecules in cytochrome bo: insights into NO reductase activity in terminal oxidases. Biochemistry. 48: 883-90. PMID 19187032 DOI: 10.1021/Bi801915R |
0.696 |
|
| 2009 |
Egawa T, Lee H, Gennis RB, Yeh S, Rousseau DL. Resonance Raman Investigation of the R481 Mutants of Cytochrome c Oxidase from R. sphaeroides Biophysical Journal. 96: 435a. DOI: 10.1016/J.Bpj.2008.12.2231 |
0.361 |
|
| 2009 |
Cvetkov TL, Gennis RB, Prochaska LJ. Functionality of Single-Cysteine Mutants in Subunit III of Rhodobacter sphaeroides Cytochrome c Oxidase Biophysical Journal. 96: 238a. DOI: 10.1016/J.Bpj.2008.12.1172 |
0.472 |
|
| 2008 |
Lin MT, Samoilova RI, Gennis RB, Dikanov SA. Identification of the nitrogen donor hydrogen bonded with the semiquinone at the Q(H) site of the cytochrome bo3 from Escherichia coli. Journal of the American Chemical Society. 130: 15768-9. PMID 18983149 DOI: 10.1021/Ja805906A |
0.584 |
|
| 2008 |
Brzezinski P, Gennis RB. Cytochrome c oxidase: exciting progress and remaining mysteries. Journal of Bioenergetics and Biomembranes. 40: 521-31. PMID 18975062 DOI: 10.1007/S10863-008-9181-7 |
0.605 |
|
| 2008 |
Morgan JE, Vakkasoglu AS, Lugtenburg J, Gennis RB, Maeda A. Structural changes due to the deprotonation of the proton release group in the M-photointermediate of bacteriorhodopsin as revealed by time-resolved FTIR spectroscopy. Biochemistry. 47: 11598-605. PMID 18837559 DOI: 10.1021/Bi801405V |
0.773 |
|
| 2008 |
Yang K, Borisov VB, Konstantinov AA, Gennis RB. The fully oxidized form of the cytochrome bd quinol oxidase from E. coli does not participate in the catalytic cycle: direct evidence from rapid kinetics studies. Febs Letters. 582: 3705-9. PMID 18823983 DOI: 10.1016/J.Febslet.2008.09.038 |
0.389 |
|
| 2008 |
Smirnova IA, Zaslavsky D, Fee JA, Gennis RB, Brzezinski P. Electron and proton transfer in the ba(3) oxidase from Thermus thermophilus. Journal of Bioenergetics and Biomembranes. 40: 281-7. PMID 18752061 DOI: 10.1007/S10863-008-9157-7 |
0.654 |
|
| 2008 |
Morgan JE, Gennis RB, Maeda A. A role for internal water molecules in proton affinity changes in the Schiff base and Asp85 for one-way proton transfer in bacteriorhodopsin. Photochemistry and Photobiology. 84: 1038-45. PMID 18557823 DOI: 10.1111/J.1751-1097.2008.00377.X |
0.363 |
|
| 2008 |
Lepp H, Salomonsson L, Zhu JP, Gennis RB, Brzezinski P. Impaired proton pumping in cytochrome c oxidase upon structural alteration of the D pathway. Biochimica Et Biophysica Acta. 1777: 897-903. PMID 18457654 DOI: 10.1016/J.Bbabio.2008.04.013 |
0.746 |
|
| 2008 |
Kikukawa T, Saha CK, Balashov SP, Imasheva ES, Zaslavsky D, Gennis RB, Abe T, Kamo N. The lifetimes of Pharaonis phoborhodopsin signaling states depend on the rates of proton transfers--effects of hydrostatic pressure and stopped flow experiments. Photochemistry and Photobiology. 84: 880-8. PMID 18346087 DOI: 10.1111/J.1751-1097.2008.00318.X |
0.342 |
|
| 2008 |
Friedrich MG, Kirste VU, Zhu J, Gennis RB, Knoll W, Naumann RL. Activity of membrane proteins immobilized on surfaces as a function of packing density. The Journal of Physical Chemistry. B. 112: 3193-201. PMID 18281973 DOI: 10.1021/Jp709717K |
0.51 |
|
| 2008 |
Li Y, Berthold DA, Gennis RB, Rienstra CM. Chemical shift assignment of the transmembrane helices of DsbB, a 20-kDa integral membrane enzyme, by 3D magic-angle spinning NMR spectroscopy. Protein Science : a Publication of the Protein Society. 17: 199-204. PMID 18227427 DOI: 10.1110/Ps.073225008 |
0.403 |
|
| 2008 |
Arutyunyan AM, Borisov VB, Novoderezhkin VI, Ghaim J, Zhang J, Gennis RB, Konstantinov AA. Strong excitonic interactions in the oxygen-reducing site of bd-type oxidase: the Fe-to-Fe distance between hemes d and b595 is 10 A. Biochemistry. 47: 1752-9. PMID 18205406 DOI: 10.1021/Bi701884G |
0.376 |
|
| 2008 |
Hemp J, Gennis RB. Diversity of the heme-copper superfamily in archaea: insights from genomics and structural modeling. Results and Problems in Cell Differentiation. 45: 1-31. PMID 18183358 DOI: 10.1007/400_2007_046 |
0.338 |
|
| 2008 |
Millett F, Brand SE, Rajagukguk S, Ganesan K, Geren L, Fabian M, Han D, Gennis RB, Durham B, Ferguson-Miller S, Mills DA. C2/2 Rapid kinetic studies of electron transfer in cytochrome oxidase Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 1777: S109. DOI: 10.1016/J.Bbabio.2008.05.428 |
0.651 |
|
| 2008 |
Yap LL, Samoilova RI, Lin MT, Gennis RB, Dikanov SA. S11.34 The semiquinone at the QH site of the cytochrome bo3 from Escherichia coli Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 1777: S73. DOI: 10.1016/J.Bbabio.2008.05.289 |
0.767 |
|
| 2008 |
Teutloff C, White G, Gennis RB, Thomson AJ, MacMillan F. S11.8 The coupling of electron and proton transfer in haem copper oxidases as studied by peldor spectroscopy Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 1777: S67. DOI: 10.1016/J.Bbabio.2008.05.263 |
0.353 |
|
| 2008 |
Gennis RB. P/21 The proton pumping heme-copper oxidases Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 1777: S7. DOI: 10.1016/J.Bbabio.2008.05.033 |
0.338 |
|
| 2007 |
Brand SE, Rajagukguk S, Ganesan K, Geren L, Fabian M, Han D, Gennis RB, Durham B, Millett F. A new ruthenium complex to study single-electron reduction of the pulsed O(H) state of detergent-solubilized cytochrome oxidase. Biochemistry. 46: 14610-8. PMID 18027981 DOI: 10.1021/Bi701424D |
0.671 |
|
| 2007 |
Szundi I, Ray J, Pawate A, Gennis RB, Einarsdóttir O. Flash-photolysis of fully reduced and mixed-valence CO-bound Rhodobacter sphaeroides cytochrome c oxidase: heme spectral shifts. Biochemistry. 46: 12568-78. PMID 17929941 DOI: 10.1021/Bi700728G |
0.751 |
|
| 2007 |
Hemp J, Han H, Roh JH, Kaplan S, Martinez TJ, Gennis RB. Comparative genomics and site-directed mutagenesis support the existence of only one input channel for protons in the C-family (cbb3 oxidase) of heme-copper oxygen reductases. Biochemistry. 46: 9963-72. PMID 17676874 DOI: 10.1021/Bi700659Y |
0.627 |
|
| 2007 |
Yang K, Zhang J, Vakkasoglu AS, Hielscher R, Osborne JP, Hemp J, Miyoshi H, Hellwig P, Gennis RB. Glutamate 107 in subunit I of the cytochrome bd quinol oxidase from Escherichia coli is protonated and near the heme d/heme b595 binuclear center. Biochemistry. 46: 3270-8. PMID 17305364 DOI: 10.1021/Bi061946+ |
0.823 |
|
| 2007 |
Morgan JE, Vakkasoglu AS, Gennis RB, Maeda A. Water structural changes in the L and M photocycle intermediates of bacteriorhodopsin as revealed by time-resolved step-scan Fourier transform infrared (FTIR) spectroscopy. Biochemistry. 46: 2787-96. PMID 17300175 DOI: 10.1021/Bi0616596 |
0.762 |
|
| 2007 |
White GF, Field S, Marritt S, Oganesyan VS, Gennis RB, Yap LL, Katsonouri A, Thomson AJ. An EPR spin label study of the quinol oxidase, E. coli cytochrome bo3: a search for redox induced conformational changes. Biochemistry. 46: 2355-63. PMID 17288457 DOI: 10.1021/Bi062265H |
0.813 |
|
| 2007 |
Li Y, Berthold DA, Frericks HL, Gennis RB, Rienstra CM. Partial (13)C and (15)N chemical-shift assignments of the disulfide-bond-forming enzyme DsbB by 3D magic-angle spinning NMR spectroscopy. Chembiochem : a European Journal of Chemical Biology. 8: 434-42. PMID 17285659 DOI: 10.1002/Cbic.200600484 |
0.403 |
|
| 2007 |
Yap LL, Samoilova RI, Gennis RB, Dikanov SA. Characterization of mutants that change the hydrogen bonding of the semiquinone radical at the QH site of the cytochrome bo3 from Escherichia coli. The Journal of Biological Chemistry. 282: 8777-85. PMID 17267395 DOI: 10.1074/Jbc.M611595200 |
0.743 |
|
| 2006 |
Hemp J, Robinson DE, Ganesan KB, Martinez TJ, Kelleher NL, Gennis RB. Evolutionary migration of a post-translationally modified active-site residue in the proton-pumping heme-copper oxygen reductases. Biochemistry. 45: 15405-10. PMID 17176062 DOI: 10.1021/Bi062026U |
0.628 |
|
| 2006 |
Han D, Namslauer A, Pawate A, Morgan JE, Nagy S, Vakkasoglu AS, Brzezinski P, Gennis RB. Replacing Asn207 by aspartate at the neck of the D channel in the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides results in decoupling the proton pump. Biochemistry. 45: 14064-74. PMID 17115701 DOI: 10.1021/Bi061465Q |
0.819 |
|
| 2006 |
Frericks HL, Zhou DH, Yap LL, Gennis RB, Rienstra CM. Magic-angle spinning solid-state NMR of a 144 kDa membrane protein complex: E. coli cytochrome bo3 oxidase. Journal of Biomolecular Nmr. 36: 55-71. PMID 16964530 DOI: 10.1007/S10858-006-9070-5 |
0.737 |
|
| 2006 |
Siletsky SA, Han D, Brand S, Morgan JE, Fabian M, Geren L, Millett F, Durham B, Konstantinov AA, Gennis RB. Single-electron photoreduction of the P(M) intermediate of cytochrome c oxidase. Biochimica Et Biophysica Acta. 1757: 1122-32. PMID 16938268 DOI: 10.1016/J.Bbabio.2006.07.003 |
0.505 |
|
| 2006 |
Vakkasoglu AS, Morgan JE, Han D, Pawate AS, Gennis RB. Mutations which decouple the proton pump of the cytochrome c oxidase from Rhodobacter sphaeroides perturb the environment of glutamate 286. Febs Letters. 580: 4613-7. PMID 16890226 DOI: 10.1016/J.Febslet.2006.07.036 |
0.81 |
|
| 2006 |
Brändén G, Gennis RB, Brzezinski P. Transmembrane proton translocation by cytochrome c oxidase. Biochimica Et Biophysica Acta. 1757: 1052-63. PMID 16824482 DOI: 10.1016/J.Bbabio.2006.05.020 |
0.636 |
|
| 2006 |
Maeda A, Morgan JE, Gennis RB, Ebrey TG. Water as a cofactor in the unidirectional light-driven proton transfer steps in bacteriorhodopsin. Photochemistry and Photobiology. 82: 1398-405. PMID 16634652 DOI: 10.1562/2006-01-16-Ir-779 |
0.348 |
|
| 2006 |
Yap LL, Samoilova RI, Gennis RB, Dikanov SA. Characterization of the exchangeable protons in the immediate vicinity of the semiquinone radical at the QH site of the cytochrome bo3 from Escherichia coli. The Journal of Biological Chemistry. 281: 16879-87. PMID 16624801 DOI: 10.1074/Jbc.M602544200 |
0.751 |
|
| 2006 |
Miksovska J, Gennis RB, Larsen RW. Thermodynamics of carbon monoxide photodissociation from the fully reduced cytochrome aa3 oxidase from Rb. sphaeroides. Biochimica Et Biophysica Acta. 1757: 182-8. PMID 16545339 DOI: 10.1016/J.Bbabio.2006.01.008 |
0.338 |
|
| 2006 |
Jeuken LJ, Connell SD, Henderson PJ, Gennis RB, Evans SD, Bushby RJ. Redox enzymes in tethered membranes. Journal of the American Chemical Society. 128: 1711-6. PMID 16448146 DOI: 10.1021/Ja056972U |
0.352 |
|
| 2006 |
Brändén G, Pawate AS, Gennis RB, Brzezinski P. Controlled uncoupling and recoupling of proton pumping in cytochrome c oxidase. Proceedings of the National Academy of Sciences of the United States of America. 103: 317-22. PMID 16407159 DOI: 10.1073/Pnas.0507734103 |
0.828 |
|
| 2005 |
Han D, Morgan JE, Gennis RB. G204D, a mutation that blocks the proton-conducting D-channel of the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides. Biochemistry. 44: 12767-74. PMID 16171391 DOI: 10.1021/Bi051141M |
0.575 |
|
| 2005 |
Hemp J, Christian C, Barquera B, Gennis RB, Martínez TJ. Helix switching of a key active-site residue in the cytochrome cbb3 oxidases. Biochemistry. 44: 10766-75. PMID 16086579 DOI: 10.1021/Bi050464F |
0.409 |
|
| 2005 |
Miksovská J, Gennis RB, Larsen RW. Photothermal studies of CO photodissociation from mixed valence Escherichia coli cytochrome bo3. Febs Letters. 579: 3014-8. PMID 15896790 DOI: 10.1016/J.Febslet.2005.04.055 |
0.338 |
|
| 2005 |
Maeda A, Gennis RB, Balashov SP, Ebrey TG. Relocation of water molecules between the Schiff base and the Thr46-Asp96 region during light-driven unidirectional proton transport by bacteriorhodopsin: an FTIR study of the N intermediate. Biochemistry. 44: 5960-8. PMID 15835885 DOI: 10.1021/Bi047469H |
0.321 |
|
| 2005 |
Belevich I, Borisov VB, Zhang J, Yang K, Konstantinov AA, Gennis RB, Verkhovsky MI. Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active site. Proceedings of the National Academy of Sciences of the United States of America. 102: 3657-62. PMID 15728392 DOI: 10.1073/Pnas.0405683102 |
0.39 |
|
| 2005 |
Riegler D, Shroyer L, Pokalsky C, Zaslavsky D, Gennis R, Prochaska LJ. Characterization of steady-state activities of cytochrome c oxidase at alkaline pH: mimicking the effect of K-channel mutations in the bovine enzyme. Biochimica Et Biophysica Acta. 1706: 126-33. PMID 15620373 DOI: 10.1016/J.Bbabio.2004.10.002 |
0.401 |
|
| 2005 |
Toepke MW, Brewer SH, Morgan JE, Vu DM, Ganesan K, Rector KD, Woodruff WH, Gennis RB, Dyer RB, Kenis PJA. Protein kinetics via spectroscopic imaging on a microfluidic chip Aiche Annual Meeting, Conference Proceedings. 12694. |
0.424 |
|
| 2005 |
Toepke MW, Brewer SH, Vu DM, Morgan JE, Ganesan K, Rector KD, Woodruff WH, Gennis RB, Dyer RB, Kenis PJA. Protein kinetics via UV/VIS and FTIR imaging on chip Micro Total Analysis Systems - Proceedings of Microtas 2005 Conference: 9th International Conference On Miniaturized Systems For Chemistry and Life Sciences. 1: 1464-1466. |
0.426 |
|
| 2004 |
Zhang J, Hellwig P, Osborne JP, Gennis RB. Arginine 391 in subunit I of the cytochrome bd quinol oxidase from Escherichia coli stabilizes the reduced form of the hemes and is essential for quinol oxidase activity. The Journal of Biological Chemistry. 279: 53980-7. PMID 15475358 DOI: 10.1074/Jbc.M408626200 |
0.425 |
|
| 2004 |
Siletsky SA, Pawate AS, Weiss K, Gennis RB, Konstantinov AA. Transmembrane charge separation during the ferryl-oxo -> oxidized transition in a nonpumping mutant of cytochrome c oxidase. The Journal of Biological Chemistry. 279: 52558-65. PMID 15385565 DOI: 10.1074/Jbc.M407549200 |
0.767 |
|
| 2004 |
Barquera B, Nilges MJ, Morgan JE, Ramirez-Silva L, Zhou W, Gennis RB. Mutagenesis study of the 2Fe-2S center and the FAD binding site of the Na(+)-translocating NADH:ubiquinone oxidoreductase from Vibrio cholerae. Biochemistry. 43: 12322-30. PMID 15379571 DOI: 10.1021/Bi048689Y |
0.563 |
|
| 2004 |
Salomonsson L, Lee A, Gennis RB, Brzezinski P. A single-amino-acid lid renders a gas-tight compartment within a membrane-bound transporter. Proceedings of the National Academy of Sciences of the United States of America. 101: 11617-21. PMID 15289603 DOI: 10.1073/Pnas.0402242101 |
0.587 |
|
| 2004 |
Zaslavsky D, Sadoski RC, Rajagukguk S, Geren L, Millett F, Durham B, Gennis RB. Direct measurement of proton release by cytochrome c oxidase in solution during the F-->O transition. Proceedings of the National Academy of Sciences of the United States of America. 101: 10544-7. PMID 15247424 DOI: 10.1073/Pnas.0401521101 |
0.465 |
|
| 2004 |
McMahon BH, Fabian M, Tomson F, Causgrove TP, Bailey JA, Rein FN, Dyer RB, Palmer G, Gennis RB, Woodruff WH. FTIR studies of internal proton transfer reactions linked to inter-heme electron transfer in bovine cytochrome c oxidase. Biochimica Et Biophysica Acta. 1655: 321-31. PMID 15100047 DOI: 10.1016/J.Bbabio.2004.01.007 |
0.772 |
|
| 2004 |
Zhang J, Barquera B, Gennis RB. Gene fusions with beta-lactamase show that subunit I of the cytochrome bd quinol oxidase from E. coli has nine transmembrane helices with the O2 reactive site near the periplasmic surface. Febs Letters. 561: 58-62. PMID 15013751 DOI: 10.1016/S0014-5793(04)00125-5 |
0.351 |
|
| 2004 |
Zhang J, Osborne JP, Gennis RB, Wang X. Proton NMR study of the heme environment in bacterial quinol oxidases. Archives of Biochemistry and Biophysics. 421: 186-91. PMID 14984198 DOI: 10.1016/J.Abb.2003.11.016 |
0.377 |
|
| 2004 |
Gennis RB. Coupled proton and electron transfer reactions in cytochrome oxidase. Frontiers in Bioscience : a Journal and Virtual Library. 9: 581-91. PMID 14766393 DOI: 10.2741/1237 |
0.403 |
|
| 2003 |
Namslauer A, Pawate AS, Gennis RB, Brzezinski P. Redox-coupled proton translocation in biological systems: proton shuttling in cytochrome c oxidase. Proceedings of the National Academy of Sciences of the United States of America. 100: 15543-7. PMID 14676323 DOI: 10.1073/Pnas.2432106100 |
0.825 |
|
| 2003 |
Maeda A, Herzfeld J, Belenky M, Needleman R, Gennis RB, Balashov SP, Ebrey TG. Water-mediated hydrogen-bonded network on the cytoplasmic side of the Schiff base of the L photointermediate of bacteriorhodopsin. Biochemistry. 42: 14122-9. PMID 14640679 DOI: 10.1021/Bi0301542 |
0.347 |
|
| 2003 |
Gennis RB. Some recent contributions of FTIR difference spectroscopy to the study of cytochrome oxidase. Febs Letters. 555: 2-7. PMID 14630310 DOI: 10.1016/S0014-5793(03)01150-5 |
0.315 |
|
| 2003 |
Nyquist RM, Heitbrink D, Bolwien C, Gennis RB, Heberle J. Direct observation of protonation reactions during the catalytic cycle of cytochrome c oxidase. Proceedings of the National Academy of Sciences of the United States of America. 100: 8715-20. PMID 12851460 DOI: 10.1073/Pnas.1530408100 |
0.83 |
|
| 2003 |
Ching E, Gennis RB, Larsen RW. Kinetics of intramolecular electron transfer in cytochrome bo3 from Escherichia coli. Biophysical Journal. 84: 2728-33. PMID 12668481 DOI: 10.1016/S0006-3495(03)75078-4 |
0.385 |
|
| 2003 |
Maeda A, Tomson FL, Gennis RB, Balashov SP, Ebrey TG. Water molecule rearrangements around Leu93 and Trp182 in the formation of the L intermediate in bacteriorhodopsin's photocycle. Biochemistry. 42: 2535-41. PMID 12614147 DOI: 10.1021/Bi020532N |
0.74 |
|
| 2003 |
Tomson FL, Morgan JE, Gu G, Barquera B, Vygodina TV, Gennis RB. Substitutions for glutamate 101 in subunit II of cytochrome c oxidase from Rhodobacter sphaeroides result in blocking the proton-conducting K-channel. Biochemistry. 42: 1711-7. PMID 12578386 DOI: 10.1021/Bi026750Y |
0.761 |
|
| 2003 |
Barquera B, Morgan JE, Lukoyanov D, Scholes CP, Gennis RB, Nilges MJ. X- and W-band EPR and Q-band ENDOR studies of the flavin radical in the Na+ -translocating NADH:quinone oxidoreductase from Vibrio cholerae. Journal of the American Chemical Society. 125: 265-75. PMID 12515529 DOI: 10.1021/Ja0207201 |
0.375 |
|
| 2002 |
Tomson F, Bailey JA, Gennis RB, Unkefer CJ, Li Z, Silks LA, Martinez RA, Donohoe RJ, Dyer RB, Woodruff WH. Direct infrared detection of the covalently ring linked His-Tyr structure in the active site of the heme-copper oxidases. Biochemistry. 41: 14383-90. PMID 12450405 DOI: 10.1021/Bi026370C |
0.757 |
|
| 2002 |
Pawate AS, Morgan J, Namslauer A, Mills D, Brzezinski P, Ferguson-Miller S, Gennis RB. A mutation in subunit I of cytochrome oxidase from Rhodobacter sphaeroides results in an increase in steady-state activity but completely eliminates proton pumping. Biochemistry. 41: 13417-23. PMID 12416987 DOI: 10.1021/Bi026582+ |
0.821 |
|
| 2002 |
Ching E, Gennis R, Larsen R. Activation volumes for intramolecular electron transfer in Escherichia coli cytochrome bo(3). Febs Letters. 527: 81-5. PMID 12220638 DOI: 10.1016/S0014-5793(02)03170-8 |
0.363 |
|
| 2002 |
Brändén M, Tomson F, Gennis RB, Brzezinski P. The entry point of the K-proton-transfer pathway in cytochrome c oxidase. Biochemistry. 41: 10794-8. PMID 12196018 DOI: 10.1021/Bi026093+ |
0.815 |
|
| 2002 |
Hellwig P, Yano T, Ohnishi T, Gennis RB. Identification of the residues involved in stabilization of the semiquinone radical in the high-affinity ubiquinone binding site in cytochrome bo(3) from Escherichia coli by site-directed mutagenesis and EPR spectroscopy. Biochemistry. 41: 10675-9. PMID 12186553 DOI: 10.1021/Bi012146W |
0.403 |
|
| 2002 |
Barquera B, Zhou W, Morgan JE, Gennis RB. Riboflavin is a component of the Na+-pumping NADH-quinone oxidoreductase from Vibrio cholerae. Proceedings of the National Academy of Sciences of the United States of America. 99: 10322-4. PMID 12122213 DOI: 10.1073/Pnas.162361299 |
0.551 |
|
| 2002 |
Hellwig P, Pfitzner U, Behr J, Rost B, Pesavento RP, Donk WV, Gennis RB, Michel H, Ludwig B, Mäntele W. Vibrational modes of tyrosines in cytochrome c oxidase from Paracoccus denitrificans: FTIR and electrochemical studies on Tyr-D4-labeled and on Tyr280His and Tyr35Phe mutant enzymes. Biochemistry. 41: 9116-25. PMID 12119026 DOI: 10.1021/Bi012056R |
0.407 |
|
| 2002 |
Lee A, Kirichenko A, Vygodina T, Siletsky SA, Das TK, Rousseau DL, Gennis R, Konstantinov AA. Ca(2+)-binding site in Rhodobacter sphaeroides cytochrome C oxidase. Biochemistry. 41: 8886-98. PMID 12102631 DOI: 10.1021/Bi020183X |
0.332 |
|
| 2002 |
Zhang J, Oettmeier W, Gennis RB, Hellwig P. FTIR spectroscopic evidence for the involvement of an acidic residue in quinone binding in cytochrome bd from Escherichia coli. Biochemistry. 41: 4612-7. PMID 11926823 DOI: 10.1021/Bi011784B |
0.395 |
|
| 2002 |
Maeda A, Balashov SP, Lugtenburg J, Verhoeven MA, Herzfeld J, Belenky M, Gennis RB, Tomson FL, Ebrey TG. Interaction of internal water molecules with the schiff base in the L intermediate of the bacteriorhodopsin photocycle. Biochemistry. 41: 3803-9. PMID 11888299 DOI: 10.1021/Bi011923P |
0.738 |
|
| 2002 |
Barquera B, Hellwig P, Zhou W, Morgan JE, Häse CC, Gosink KK, Nilges M, Bruesehoff PJ, Roth A, Lancaster CR, Gennis RB. Purification and characterization of the recombinant Na(+)-translocating NADH:quinone oxidoreductase from Vibrio cholerae. Biochemistry. 41: 3781-9. PMID 11888296 DOI: 10.1021/Bi011873O |
0.568 |
|
| 2002 |
Bailey JA, Tomson FL, Mecklenburg SL, MacDonald GM, Katsonouri A, Puustinen A, Gennis RB, Woodruff WH, Dyer RB. Time-resolved step-scan Fourier transform infrared spectroscopy of the CO adducts of bovine cytochrome c oxidase and of cytochrome bo(3) from Escherichia coli. Biochemistry. 41: 2675-83. PMID 11851414 DOI: 10.1021/Bi010823G |
0.82 |
|
| 2002 |
Borisov VB, Liebl U, Rappaport F, Martin JL, Zhang J, Gennis RB, Konstantinov AA, Vos MH. Interactions between heme d and heme b595 in quinol oxidase bd from Escherichia coli: a photoselection study using femtosecond spectroscopy. Biochemistry. 41: 1654-62. PMID 11814360 DOI: 10.1021/Bi0158019 |
0.398 |
|
| 2001 |
Pecoraro C, Gennis RB, Vygodina TV, Konstantinov AA. Role of the K-channel in the pH-dependence of the reaction of cytochrome c oxidase with hydrogen peroxide. Biochemistry. 40: 9695-708. PMID 11583170 DOI: 10.1021/Bi010115V |
0.819 |
|
| 2001 |
Nyquist RM, Heitbrink D, Bolwien C, Wells TA, Gennis RB, Heberle J. Perfusion-induced redox differences in cytochrome c oxidase: ATR/FT-IR spectroscopy. Febs Letters. 505: 63-7. PMID 11557043 DOI: 10.1016/S0014-5793(01)02769-7 |
0.795 |
|
| 2001 |
Zhang J, Hellwig P, Osborne JP, Huang HW, Moënne-Loccoz P, Konstantinov AA, Gennis RB. Site-directed mutation of the highly conserved region near the Q-loop of the cytochrome bd quinol oxidase from Escherichia coli specifically perturbs heme b595. Biochemistry. 40: 8548-56. PMID 11456494 DOI: 10.1021/Bi010469M |
0.408 |
|
| 2001 |
Das TK, Tomson FL, Gennis RB, Gordon M, Rousseau DL. pH-dependent structural changes at the Heme-Copper binuclear center of cytochrome c oxidase. Biophysical Journal. 80: 2039-45. PMID 11325707 DOI: 10.1016/S0006-3495(01)76177-2 |
0.772 |
|
| 2001 |
Brändén M, Sigurdson H, Namslauer A, Gennis RB, Adelroth P, Brzezinski P. On the role of the K-proton transfer pathway in cytochrome c oxidase. Proceedings of the National Academy of Sciences of the United States of America. 98: 5013-8. PMID 11296255 DOI: 10.1073/Pnas.081088398 |
0.646 |
|
| 2001 |
Barquera B, Häse CC, Gennis RB. Expression and mutagenesis of the NqrC subunit of the NQR respiratory Na(+) pump from Vibrio cholerae with covalently attached FMN. Febs Letters. 492: 45-9. PMID 11248234 DOI: 10.1016/S0014-5793(01)02224-4 |
0.352 |
|
| 2001 |
Hellwig P, Barquera B, Gennis RB. Direct evidence for the protonation of aspartate-75, proposed to be at a quinol binding site, upon reduction of cytochrome bo3 from Escherichia coli. Biochemistry. 40: 1077-82. PMID 11170431 DOI: 10.1021/Bi002154X |
0.47 |
|
| 2000 |
Adelroth P, Karpefors M, Gilderson G, Tomson FL, Gennis RB, Brzezinski P. Proton transfer from glutamate 286 determines the transition rates between oxygen intermediates in cytochrome c oxidase. Biochimica Et Biophysica Acta. 1459: 533-9. PMID 11004473 DOI: 10.1016/S0005-2728(00)00194-8 |
0.815 |
|
| 2000 |
Maeda A, Tomson FL, Gennis RB, Kandori H, Ebrey TG, Balashov SP. Relocation of internal bound water in bacteriorhodopsin during the photoreaction of M at low temperatures: an FTIR study. Biochemistry. 39: 10154-62. PMID 10956004 DOI: 10.1021/Bi000190Q |
0.725 |
|
| 2000 |
Zaslavsky D, Gennis RB. Proton pumping by cytochrome oxidase: progress, problems and postulates. Biochimica Et Biophysica Acta. 1458: 164-79. PMID 10812031 DOI: 10.1016/S0005-2728(00)00066-9 |
0.473 |
|
| 2000 |
Veselov AV, Osborne JP, Gennis RB, Scholes CP. Q-band ENDOR (electron nuclear double resonance) of the high-affinity ubisemiquinone center in cytochrome bo3 from Escherichia coli. Biochemistry. 39: 3169-75. PMID 10715139 DOI: 10.1021/Bi9926835 |
0.373 |
|
| 2000 |
Lee HM, Das TK, Rousseau DL, Mills D, Ferguson-Miller S, Gennis RB. Mutations in the putative H-channel in the cytochrome c oxidase from Rhodobacter sphaeroides show that this channel is not important for proton conduction but reveal modulation of the properties of heme a. Biochemistry. 39: 2989-96. PMID 10715119 DOI: 10.1021/Bi9924821 |
0.577 |
|
| 2000 |
Veselov AV, Osborne JP, Gennis RB, Scholes CP. Q-band ENDOR (electron nuclear double resonance) of the heme o3 liganding environment at the binuclear center in cytochrome bo3 from Escherichia coli Journal of the American Chemical Society. 122: 8712-8716. DOI: 10.1021/Ja000688F |
0.328 |
|
| 1999 |
Zaslavsky D, Smirnova IA, Brzezinski P, Shinzawa-Itoh K, Yoshikawa S, Gennis RB. Examination of the reaction of fully reduced cytochrome oxidase with hydrogen peroxide by flow-flash spectroscopy. Biochemistry. 38: 16016-23. PMID 10625470 DOI: 10.1021/Bi9916675 |
0.591 |
|
| 1999 |
Crofts AR, Barquera B, Gennis RB, Kuras R, Guergova-Kuras M, Berry EA. Mechanism of ubiquinol oxidation by the bc(1) complex: different domains of the quinol binding pocket and their role in the mechanism and binding of inhibitors. Biochemistry. 38: 15807-26. PMID 10625446 DOI: 10.1021/Bi990962M |
0.375 |
|
| 1999 |
Zhou W, Bertsova YV, Feng B, Tsatsos P, Verkhovskaya ML, Gennis RB, Bogachev AV, Barquera B. Sequencing and preliminary characterization of the Na+-translocating NADH:ubiquinone oxidoreductase from Vibrio harveyi. Biochemistry. 38: 16246-52. PMID 10587447 DOI: 10.1021/Bi991664S |
0.511 |
|
| 1999 |
Gennis RB, Ebrey TG. Proton pump caught in the act. Science (New York, N.Y.). 286: 252-3. PMID 10577192 DOI: 10.1126/Science.286.5438.252 |
0.35 |
|
| 1999 |
Ma J, Tsatsos PH, Zaslavsky D, Barquera B, Thomas JW, Katsonouri A, Puustinen A, Wikström M, Brzezinski P, Alben JO, Gennis RB. Glutamate-89 in subunit II of cytochrome bo3 from Escherichia coli is required for the function of the heme-copper oxidase. Biochemistry. 38: 15150-6. PMID 10563797 DOI: 10.1021/Bi991764Y |
0.796 |
|
| 1999 |
Fabian M, Wong WW, Gennis RB, Palmer G. Mass spectrometric determination of dioxygen bond splitting in the "peroxy" intermediate of cytochrome c oxidase. Proceedings of the National Academy of Sciences of the United States of America. 96: 13114-7. PMID 10557282 DOI: 10.1073/Pnas.96.23.13114 |
0.352 |
|
| 1999 |
Hellwig P, Mogi T, Tomson FL, Gennis RB, Iwata J, Miyoshi H, Mäntele W. Vibrational modes of ubiquinone in cytochrome bo(3) from Escherichia coli identified by Fourier transform infrared difference spectroscopy and specific (13)C labeling. Biochemistry. 38: 14683-9. PMID 10545194 DOI: 10.1021/Bi991267H |
0.752 |
|
| 1999 |
Musatov A, Ortega-Lopez J, Demeler B, Osborne JP, Gennis RB, Robinson NC. Detergent-solubilized Escherichia coli cytochrome bo3 ubiquinol oxidase: a monomeric, not a dimeric complex. Febs Letters. 457: 153-6. PMID 10486584 DOI: 10.1016/S0014-5793(99)01020-0 |
0.311 |
|
| 1999 |
Crofts AR, Hong S, Ugulava N, Barquera B, Gennis R, Guergova-Kuras M, Berry EA. Pathways for proton release during ubihydroquinone oxidation by the bc(1) complex. Proceedings of the National Academy of Sciences of the United States of America. 96: 10021-6. PMID 10468555 DOI: 10.1073/Pnas.96.18.10021 |
0.438 |
|
| 1999 |
Maeda A, Tomson FL, Gennis RB, Ebrey TG, Balashov SP. Chromophore-protein-water interactions in the L intermediate of bacteriorhodopsin: FTIR study of the photoreaction of L at 80 K. Biochemistry. 38: 8800-7. PMID 10393556 DOI: 10.1021/Bi9907072 |
0.716 |
|
| 1999 |
Smirnova IA, Adelroth P, Gennis RB, Brzezinski P. Aspartate-132 in cytochrome c oxidase from Rhodobacter sphaeroides is involved in a two-step proton transfer during oxo-ferryl formation. Biochemistry. 38: 6826-33. PMID 10346904 DOI: 10.1021/Bi982865J |
0.633 |
|
| 1999 |
Osborne JP, Cosper NJ, Stälhandske CM, Scott RA, Alben JO, Gennis RB. Cu XAS shows a change in the ligation of CuB upon reduction of cytochrome bo3 from Escherichia coli. Biochemistry. 38: 4526-32. PMID 10194374 DOI: 10.1021/Bi982278Y |
0.431 |
|
| 1999 |
Guergova-Kuras M, Salcedo-Hernandez R, Bechmann G, Kuras R, Gennis RB, Crofts AR. Expression and one-step purification of a fully active polyhistidine-tagged cytochrome bc1 complex from Rhodobacter sphaeroides. Protein Expression and Purification. 15: 370-80. PMID 10092497 DOI: 10.1006/Prep.1998.1018 |
0.377 |
|
| 1999 |
Osborne JP, Gennis RB. Sequence analysis of cytochrome bd oxidase suggests a revised topology for subunit I. Biochimica Et Biophysica Acta. 1410: 32-50. PMID 10076013 DOI: 10.1016/S0005-2728(98)00171-6 |
0.394 |
|
| 1999 |
Zaslavsky D, Smirnova IA, Adelroth P, Brzezinski P, Gennis RB. Observation of a novel transient ferryl complex with reduced CuB in cytochrome c oxidase. Biochemistry. 38: 2307-11. PMID 10029523 DOI: 10.1021/Bi9822832 |
0.599 |
|
| 1999 |
Borisov V, Arutyunyan AM, Osborne JP, Gennis RB, Konstantinov AA. Magnetic circular dichroism used to examine the interaction of Escherichia coli cytochrome bd with ligands. Biochemistry. 38: 740-50. PMID 9888814 DOI: 10.1021/Bi981908T |
0.316 |
|
| 1999 |
Maeda A, Tomson FL, Gennis RB, Ebrey TG, Balashov SP. Dynamics of Internal water molecules of bacteriorhodopsin : a low temperature FTIR study. Seibutsu Butsuri. 39: S74. DOI: 10.2142/Biophys.39.S74_1 |
0.705 |
|
| 1998 |
Gennis RB. How does cytochrome oxidase pump protons? Proceedings of the National Academy of Sciences of the United States of America. 95: 12747-9. PMID 9788983 DOI: 10.1073/Pnas.95.22.12747 |
0.374 |
|
| 1998 |
Zaslavsky D, Sadoski RC, Wang K, Durham B, Gennis RB, Millett F. Single electron reduction of cytochrome c oxidase compound F: resolution of partial steps by transient spectroscopy. Biochemistry. 37: 14910-6. PMID 9778367 DOI: 10.1021/Bi981490Z |
0.388 |
|
| 1998 |
Das TK, Pecoraro C, Tomson FL, Gennis RB, Rousseau DL. The post-translational modification in cytochrome c oxidase is required to establish a functional environment of the catalytic site. Biochemistry. 37: 14471-6. PMID 9772174 DOI: 10.1021/Bi981500W |
0.803 |
|
| 1998 |
Ma J, Puustinen A, Wikström M, Gennis RB. Tryptophan-136 in subunit II of cytochrome bo3 from Escherichia coli may participate in the binding of ubiquinol. Biochemistry. 37: 11806-11. PMID 9718303 DOI: 10.1021/Bi9809977 |
0.416 |
|
| 1998 |
Toledo-Cuevas M, Barquera B, Gennis RB, Wikström M, García-Horsman JA. The cbb3-type cytochrome c oxidase from Rhodobacter sphaeroides, a proton-pumping heme-copper oxidase. Biochimica Et Biophysica Acta. 1365: 421-34. PMID 9711295 DOI: 10.1016/S0005-2728(98)00095-4 |
0.361 |
|
| 1998 |
Hastings SF, Kaysser TM, Jiang F, Salerno JC, Gennis RB, Ingledew WJ. Identification of a stable semiquinone intermediate in the purified and membrane bound ubiquinol oxidase-cytochrome bd from Escherichia coli. European Journal of Biochemistry / Febs. 255: 317-23. PMID 9692934 |
0.314 |
|
| 1998 |
Tsatsos PH, Reynolds K, Nickels EF, He DY, Yu CA, Gennis RB. Using matrix-assisted laser desorption ionization mass spectrometry to map the quinol binding site of cytochrome bo3 from Escherichia coli. Biochemistry. 37: 9884-8. PMID 9665692 DOI: 10.1021/Bi9809270 |
0.312 |
|
| 1998 |
Gennis RB. Cytochrome c oxidase: one enzyme, two mechanisms? Science (New York, N.Y.). 280: 1712-3. PMID 9660711 DOI: 10.1126/Science.280.5370.1712 |
0.359 |
|
| 1998 |
Vibat CR, Cecchini G, Nakamura K, Kita K, Gennis RB. Localization of histidine residues responsible for heme axial ligation in cytochrome b556 of complex II (succinate:ubiquinone oxidoreductase) in Escherichia coli. Biochemistry. 37: 4148-59. PMID 9521736 DOI: 10.1021/Bi9716635 |
0.374 |
|
| 1998 |
Zaslavsky D, Gennis RB. Substitution of lysine-362 in a putative proton-conducting channel in the cytochrome c oxidase from Rhodobacter sphaeroides blocks turnover with O2 but not with H2O2. Biochemistry. 37: 3062-7. PMID 9485459 DOI: 10.1021/Bi971877M |
0.464 |
|
| 1998 |
Vygodina TV, Pecoraro C, Mitchell D, Gennis R, Konstantinov AA. Mechanism of inhibition of electron transfer by amino acid replacement K362M in a proton channel of Rhodobacter sphaeroides cytochrome c oxidase. Biochemistry. 37: 3053-61. PMID 9485458 DOI: 10.1021/Bi971876U |
0.818 |
|
| 1998 |
Adelroth P, Gennis RB, Brzezinski P. Role of the pathway through K(I-362) in proton transfer in cytochrome c oxidase from R. sphaeroides. Biochemistry. 37: 2470-6. PMID 9485395 DOI: 10.1021/Bi971813B |
0.647 |
|
| 1998 |
Gennis RB. Multiple proton-conducting pathways in cytochrome oxidase and a proposed role for the active-site tyrosine Biochimica Et Biophysica Acta - Bioenergetics. 1365: 241-248. DOI: 10.1016/S0005-2728(98)00075-9 |
0.432 |
|
| 1997 |
Ghaim JB, Tsatsos PH, Katsonouri A, Mitchell DM, Salcedo-Hernandez R, Gennis RB. Matrix-assisted laser desorption ionization mass spectrometry of membrane proteins: demonstration of a simple method to determine subunit molecular weights of hydrophobic subunits. Biochimica Et Biophysica Acta. 1330: 113-20. PMID 9408163 DOI: 10.1016/S0005-2736(97)00127-2 |
0.688 |
|
| 1997 |
Jünemann S, Meunier B, Gennis RB, Rich PR. Effects of mutation of the conserved lysine-362 in cytochrome c oxidase from Rhodobacter sphaeroides. Biochemistry. 36: 14456-64. PMID 9398164 DOI: 10.1021/Bi971458P |
0.488 |
|
| 1997 |
Adelroth P, Ek MS, Mitchell DM, Gennis RB, Brzezinski P. Glutamate 286 in cytochrome aa3 from Rhodobacter sphaeroides is involved in proton uptake during the reaction of the fully-reduced enzyme with dioxygen. Biochemistry. 36: 13824-9. PMID 9374859 DOI: 10.1021/Bi9629079 |
0.652 |
|
| 1997 |
Watmough NJ, Katsonouri A, Little RH, Osborne JP, Furlong-Nickels E, Gennis RB, Brittain T, Greenwood C. A conserved glutamic acid in helix VI of cytochrome bo3 influences a key step in oxygen reduction. Biochemistry. 36: 13736-42. PMID 9354645 DOI: 10.1021/Bi971434I |
0.753 |
|
| 1997 |
Adelroth P, Mitchell DM, Gennis RB, Brzezinski P. Factors determining electron-transfer rates in cytochrome c oxidase: studies of the FQ(I-391) mutant of the Rhodobacter sphaeroides enzyme. Biochemistry. 36: 11787-96. PMID 9305969 DOI: 10.1021/Bi962824S |
0.624 |
|
| 1997 |
Ma J, Katsonouri A, Gennis RB. Subunit II of the cytochrome bo3 ubiquinol oxidase from Escherichia coli is a lipoprotein. Biochemistry. 36: 11298-303. PMID 9298948 DOI: 10.1021/Bi9709710 |
0.712 |
|
| 1997 |
Konstantinov AA, Siletsky S, Mitchell D, Kaulen A, Gennis RB. The roles of the two proton input channels in cytochrome c oxidase from Rhodobacter sphaeroides probed by the effects of site-directed mutations on time-resolved electrogenic intraprotein proton transfer. Proceedings of the National Academy of Sciences of the United States of America. 94: 9085-90. PMID 9256439 DOI: 10.1073/Pnas.94.17.9085 |
0.454 |
|
| 1997 |
Rumbley JN, Furlong Nickels E, Gennis RB. One-step purification of histidine-tagged cytochrome bo3 from Escherichia coli and demonstration that associated quinone is not required for the structural integrity of the oxidase. Biochimica Et Biophysica Acta. 1340: 131-42. PMID 9217023 DOI: 10.1016/S0167-4838(97)00036-8 |
0.42 |
|
| 1996 |
Svensson-Ek M, Thomas JW, Gennis RB, Nilsson T, Brzezinski P. Kinetics of electron and proton transfer during the reaction of wild type and helix VI mutants of cytochrome bo3 with oxygen. Biochemistry. 35: 13673-80. PMID 8885847 DOI: 10.1021/Bi961466Q |
0.659 |
|
| 1996 |
Mitchell DM, Fetter JR, Mills DA, Adelroth P, Pressler MA, Kim Y, Aasa R, Brzezinski P, Malmström BG, Alben JO, Båbcock GT, Ferguson-Miller S, Gennis RB. Site-directed mutagenesis of residues lining a putative proton transfer pathway in cytochrome c oxidase from Rhodobacter sphaeroides. Biochemistry. 35: 13089-93. PMID 8855945 DOI: 10.1021/Bi961416L |
0.65 |
|
| 1996 |
Gennis RB, Ferguson-Miller S. Protein structure: Proton-pumping oxidases Current Biology. 6: 36-38. PMID 8825522 DOI: 10.1016/S0960-9822(02)00416-5 |
0.377 |
|
| 1996 |
Mitchell DM, Shapleigh JP, Archer AM, Alben JO, Gennis RB. A pH-dependent polarity change at the binuclear center of reduced cytochrome c oxidase detected by FTIR difference spectroscopy of the CO adduct. Biochemistry. 35: 9446-50. PMID 8755723 DOI: 10.1021/Bi960392F |
0.35 |
|
| 1996 |
Hosler JP, Shapleigh JP, Mitchell DM, Kim Y, Pressler MA, Georgiou C, Babcock GT, Alben JO, Ferguson-Miller S, Gennis RB. Polar residues in helix VIII of subunit I of cytochrome c oxidase influence the activity and the structure of the active site. Biochemistry. 35: 10776-83. PMID 8718868 DOI: 10.1021/Bi9606511 |
0.406 |
|
| 1996 |
Sun J, Kahlow MA, Kaysser TM, Osborne JP, Hill JJ, Rohlfs RJ, Hille R, Gennis RB, Loehr TM. Resonance Raman spectroscopic identification of a histidine ligand of b595 and the nature of the ligation of chlorin d in the fully reduced Escherichia coli cytochrome bd oxidase. Biochemistry. 35: 2403-12. PMID 8652583 DOI: 10.1021/Bi9518252 |
0.357 |
|
| 1996 |
Nakamura K, Yamaki M, Sarada M, Nakayama S, Vibat CR, Gennis RB, Nakayashiki T, Inokuchi H, Kojima S, Kita K. Two hydrophobic subunits are essential for the heme b ligation and functional assembly of complex II (succinate-ubiquinone oxidoreductase) from Escherichia coli. The Journal of Biological Chemistry. 271: 521-7. PMID 8550613 DOI: 10.1074/Jbc.271.1.521 |
0.374 |
|
| 1996 |
Mitchell DM, Adelroth P, Hosler JP, Fetter JR, Brzezinski P, Pressler MA, Aasa R, Malmström BG, Alben JO, Babcock GT, Gennis RB, Ferguson-Miller S. A ligand-exchange mechanism of proton pumping involving tyrosine-422 of subunit I of cytochrome oxidase is ruled out. Biochemistry. 35: 824-8. PMID 8547262 DOI: 10.1021/Bi951897T |
0.635 |
|
| 1996 |
Wang J, Rumbley J, Ching YC, Takahashi S, Gennis RB, Rousseau DL. Reaction of cytochrome bo3 with oxygen: extra redox center(s) are present in the protein. Biochemistry. 34: 15504-11. PMID 7492552 DOI: 10.1021/Bi00047A016 |
0.399 |
|
| 1996 |
Sun J, Osborne JP, Kahlow MA, Kaysser TM, Hill JJ, Gennis RB, Loehr TM. Resonance Raman Studies ofEscherichia coliCytochromebdOxidase. Selective Enhancement of the Three Heme Chromophores of the “As-Isolated” Enzyme and Characterization of the Cyanide Adduct Biochemistry. 35: 666-666. DOI: 10.1021/Bi955023I |
0.327 |
|
| 1995 |
Hill BC, Hill JJ, Gennis RB. The room temperature reaction of carbon monoxide and oxygen with the cytochrome bd quinol oxidase from Escherichia coli. Biochemistry. 33: 15110-5. PMID 7999770 DOI: 10.1021/Bi00254A021 |
0.353 |
|
| 1995 |
Peterson J, Vibat C, Gennis RB. Identification of the axial heme ligands of cytochrome b556 in succinate: ubiquinone oxidoreductase from Escherichia coli. Febs Letters. 355: 155-6. PMID 7982490 DOI: 10.1016/0014-5793(94)01189-3 |
0.365 |
|
| 1995 |
Fetter JR, Qian J, Shapleigh J, Thomas JW, García-Horsman A, Schmidt E, Hosler J, Babcock GT, Gennis RB, Ferguson-Miller S. Possible proton relay pathways in cytochrome c oxidase. Proceedings of the National Academy of Sciences of the United States of America. 92: 1604-8. PMID 7878026 DOI: 10.1073/Pnas.92.5.1604 |
0.49 |
|
| 1995 |
Svensson M, Hallén S, Thomas JW, Lemieux LJ, Gennis RB, Nilsson T. Oxygen reaction and proton uptake in helix VIII mutants of cytochrome bo3. Biochemistry. 34: 5252-8. PMID 7711046 DOI: 10.1021/Bi00015A040 |
0.436 |
|
| 1995 |
Garcia-Horsman JA, Puustinen A, Gennis RB, Wikström M. Proton transfer in cytochrome bo3 ubiquinol oxidase of Escherichia coli: second-site mutations in subunit I that restore proton pumping in the mutant Asp135-->Asn. Biochemistry. 34: 4428-33. PMID 7703256 DOI: 10.1021/bi00013a035 |
0.322 |
|
| 1995 |
Calhoun MW, Lemieux LJ, Garcia-Horsman JA, Thomas JW, Alben JO, Gennis RB. The highly conserved methionine of subunit I of the heme-copper oxidases is not at the heme-copper dinuclear center: mutagenesis of M110 in subunit I of cytochrome bo3-type ubiquinol oxidase from Escherichia coli. Febs Letters. 368: 523-5. PMID 7635213 DOI: 10.1016/0014-5793(95)00696-7 |
0.377 |
|
| 1995 |
Mitchell DM, Gennis RB. Rapid purification of wildtype and mutant cytochrome c oxidase from Rhodobacter sphaeroides by Ni(2+)-NTA affinity chromatography. Febs Letters. 368: 148-50. PMID 7615070 DOI: 10.1016/0014-5793(95)00626-K |
0.41 |
|
| 1995 |
Mitchell DM, Aasa R, Adelroth P, Brzezinski P, Gennis RB, Malmström BG. EPR studies of wild-type and several mutants of cytochrome c oxidase from Rhodobacter sphaeroides: Glu286 is not a bridging ligand in the cytochrome a3-CuB center. Febs Letters. 374: 371-4. PMID 7589573 DOI: 10.1016/0014-5793(95)01149-9 |
0.612 |
|
| 1995 |
Kaysser TM, Ghaim JB, Georgiou C, Gennis RB. Methionine-393 is an axial ligand of the heme b558 component of the cytochrome bd ubiquinol oxidase from escherichia coli Biochemistry. 34: 13491-13501. PMID 7577938 DOI: 10.1021/Bi00041A029 |
0.396 |
|
| 1995 |
Sun J, Osborne JP, Kahlow MA, Kaysser TM, Hil JJ, Gennis RB, Loehr TM. Resonance Raman studies of Escherichia coli cytochrome bd oxidase. Selective enhancement of the three heme chromophores of the "as-isolated" enzyme and characterization of the cyanide adduct. Biochemistry. 34: 12144-51. PMID 7547954 DOI: 10.1021/Bi00038A007 |
0.351 |
|
| 1995 |
Ghaim JB, Greiner DP, Meares CF, Gennis RB. Proximity mapping the surface of a membrane protein using an artificial protease: demonstration that the quinone-binding domain of subunit I is near the N-terminal region of subunit II of cytochrome bd. Biochemistry. 34: 11311-5. PMID 7547857 DOI: 10.1021/Bi00036A002 |
0.362 |
|
| 1995 |
Hirota S, Mogi T, Anraku Y, Gennis RB, Kitagawa T. Resonance raman study on axial ligands of heme irons in cytochromebd-type ubiquinol oxidase fromEscherichia coli Biospectroscopy. 1: 305-311. DOI: 10.1002/Bspy.350010502 |
0.347 |
|
| 1994 |
Cheesman MR, Watmough NJ, Gennis RB, Greenwood C, Thomson AJ. Magnetic-circular-dichroism studies of Escherichia coli cytochrome bo. Identification of high-spin ferric, low-spin ferric and ferryl [Fe(IV)] forms of heme o. European Journal of Biochemistry / Febs. 219: 595-602. PMID 8307024 DOI: 10.1111/J.1432-1033.1994.Tb19975.X |
0.344 |
|
| 1994 |
Brown S, Rumbley JN, Moody AJ, Thomas JW, Gennis RB, Rich PR. Flash photolysis of the carbon monoxide compounds of wild-type and mutant variants of cytochrome bo from Escherichia coli. Biochimica Et Biophysica Acta. 1183: 521-32. PMID 8286401 DOI: 10.1016/0005-2728(94)90080-9 |
0.404 |
|
| 1994 |
Ohnishi T, Sled VD, Rudnitzky NI, Jacobson BW, Fukumori Y, Meinhardt SW, Calhoun MW, Gennis RB, Leif H, Freidrich T, Weiss H. Biophysical and biochemical studies of bacterial NADH:quinone oxidoreductase (NDH-1) Biochemical Society Transactions. 22: 70S. PMID 8206301 DOI: 10.1042/Bst022070S |
0.353 |
|
| 1994 |
Calhoun MW, Gennis RB, Ingledew WJ, Salerno JC. Strong-field and integral spin-ligand complexes of the cytochrome bo quinol oxidase in Escherichia coli membrane preparations. Biochimica Et Biophysica Acta. 1206: 143-54. PMID 8186244 DOI: 10.1016/0167-4838(94)90083-3 |
0.37 |
|
| 1994 |
García-Horsman JA, Berry E, Shapleigh JP, Alben JO, Gennis RB. A novel cytochrome c oxidase from Rhodobacter sphaeroides that lacks CuA. Biochemistry. 33: 3113-9. PMID 8130226 DOI: 10.1021/bi00176a046 |
0.301 |
|
| 1994 |
Hosler JP, Shapleigh JP, Tecklenburg MJ, Thomas JW, Kim Y, Espe M, Fetter J, Babcock GT, Alben JO, Gennis RB. A loop between transmembrane helices IX and X of subunit I of cytochrome c oxidase caps the heme a-heme a3-CuB center. Biochemistry. 33: 1194-201. PMID 8110750 DOI: 10.1021/Bi00171A019 |
0.403 |
|
| 1994 |
Trumpower BL, Gennis RB. Energy transduction by cytochrome complexes in mitochondrial and bacterial respiration: the enzymology of coupling electron transfer reactions to transmembrane proton translocation. Annual Review of Biochemistry. 63: 675-716. PMID 7979252 DOI: 10.1146/Annurev.Bi.63.070194.003331 |
0.435 |
|
| 1994 |
Hacker B, Barquera B, Gennis RB, Crofts AR. Site-directed mutagenesis of arginine-114 and tryptophan-129 in the cytochrome b subunit of the bc1 complex of Rhodobacter sphaeroides: two highly conserved residues predicted to be near the cytoplasmic surface of putative transmembrane helices B and C. Biochemistry. 33: 13022-31. PMID 7947707 DOI: 10.1021/Bi00248A011 |
0.429 |
|
| 1994 |
Thomas JW, Calhoun MW, Lemieux LJ, Puustinen A, Wikström M, Alben JO, Gennis RB. Site-directed mutagenesis of residues within helix VI in subunit I of the cytochrome bo3 ubiquinol oxidase from Escherichia coli suggests that tyrosine 288 may be a CuB ligand. Biochemistry. 33: 13013-21. PMID 7947706 DOI: 10.1021/Bi00248A010 |
0.43 |
|
| 1994 |
Calhoun MW, Thomas JW, Gennis RB. The cytochrome oxidase superfamily of redox-driven proton pumps. Trends in Biochemical Sciences. 19: 325-30. PMID 7940677 DOI: 10.1016/0968-0004(94)90071-X |
0.42 |
|
| 1994 |
Yun C, Barquera B, Iba K, Takamiya K, Shapleigh J, Crofts AR, Gennis RB. Deletion of the gene encoding cytochromeb562fromRhodobacter sphaeroides Fems Microbiology Letters. 120: 105-110. DOI: 10.1111/J.1574-6968.1994.Tb07015.X |
0.313 |
|
| 1993 |
Hill JJ, Alben JO, Gennis RB. Spectroscopic evidence for a heme-heme binuclear center in the cytochrome bd ubiquinol oxidase from Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America. 90: 5863-7. PMID 8516338 DOI: 10.1073/Pnas.90.12.5863 |
0.405 |
|
| 1993 |
Calhoun MW, Oden KL, Gennis RB, de Mattos MJ, Neijssel OM. Energetic efficiency of Escherichia coli: effects of mutations in components of the aerobic respiratory chain. Journal of Bacteriology. 175: 3020-5. PMID 8491720 DOI: 10.1128/Jb.175.10.3020-3025.1993 |
0.4 |
|
| 1993 |
Fang H, Gennis RB. Identification of the transcriptional start site of the cyd operon from Escherichia coli. Fems Microbiology Letters. 108: 237-42. PMID 8486248 DOI: 10.1111/J.1574-6968.1993.Tb06105.X |
0.328 |
|
| 1993 |
Thomas JW, Puustinen A, Alben JO, Gennis RB, Wikström M. Substitution of asparagine for aspartate-135 in subunit I of the cytochrome bo ubiquinol oxidase of Escherichia coli eliminates proton-pumping activity. Biochemistry. 32: 10923-8. PMID 8399242 DOI: 10.1021/Bi00091A048 |
0.475 |
|
| 1993 |
Calhoun MW, Thomas JW, Hill JJ, Hosler JP, Shapleigh JP, Tecklenburg MM, Ferguson-Miller S, Babcock GT, Alben JO, Gennis RB. Identity of the axial ligand of the high-spin heme in cytochrome oxidase: spectroscopic characterization of mutants in the bo-type oxidase of Escherichia coli and the aa3-type oxidase of Rhodobacter sphaeroides. Biochemistry. 32: 10905-11. PMID 8399240 DOI: 10.1021/Bi00091A046 |
0.464 |
|
| 1993 |
Gennis RB, Barquera B, Hacker B, Van Doren SR, Arnaud S, Crofts AR, Davidson E, Gray KA, Daldal F. The bc1 complexes of Rhodobacter sphaeroides and Rhodobacter capsulatus. Journal of Bioenergetics and Biomembranes. 25: 195-209. PMID 8394316 DOI: 10.1007/Bf00762582 |
0.42 |
|
| 1993 |
Van Doren SR, Gennis RB, Barquera B, Crofts AR. Site-directed mutations of conserved residues of the Rieske iron-sulfur subunit of the cytochrome bc1 complex of Rhodobacter sphaeroides blocking or impairing quinol oxidation. Biochemistry. 32: 8083-91. PMID 8394124 DOI: 10.1021/Bi00083A005 |
0.392 |
|
| 1993 |
Ma J, Lemieux L, Gennis RB. Genetic fusion of subunits I, II, and III of the cytochrome bo ubiquinol oxidase from Escherichia coli results in a fully assembled and active enzyme. Biochemistry. 32: 7692-7. PMID 8394111 DOI: 10.1021/Bi00081A013 |
0.376 |
|
| 1993 |
Hosler JP, Ferguson-Miller S, Calhoun MW, Thomas JW, Hill J, Lemieux L, Ma J, Georgiou C, Fetter J, Shapleigh J, Tecklenburg MMJ, Babcock GT, Gennis RB. Insight into the active-site structure and function of cytochrome oxidase by analysis of site-directed mutants of bacterial cytochrome aa3 and cytochrome bo Journal of Bioenergetics and Biomembranes. 25: 121-136. PMID 8389745 DOI: 10.1007/Bf00762854 |
0.461 |
|
| 1993 |
Calhoun MW, Gennis RB. Demonstration of separate genetic loci encoding distinct membrane-bound respiratory NADH dehydrogenases in Escherichia coli. Journal of Bacteriology. 175: 3013-9. PMID 8387992 DOI: 10.1128/Jb.175.10.3013-3019.1993 |
0.372 |
|
| 1993 |
Hacker B, Barquera B, Crofts AR, Gennis RB. Characterization of mutations in the cytochrome b subunit of the bc1 complex of Rhodobacter sphaeroides that affect the quinone reductase site (Qc). Biochemistry. 32: 4403-10. PMID 8386545 DOI: 10.1021/Bi00067A033 |
0.402 |
|
| 1993 |
Watmough NJ, Cheesman MR, Gennis RB, Greenwood C, Thomson AJ. Distinct forms of the haem o-Cu binuclear site of oxidised cytochrome bo from Escherichia coli. Evidence from optical and EPR spectroscopy. Febs Letters. 319: 151-4. PMID 8384121 DOI: 10.1016/0014-5793(93)80056-Z |
0.367 |
|
| 1993 |
Moody AJ, Rumbley JN, Gennis RB, Ingledew WJ, Rich PR. Ligand-binding properties and heterogeneity of cytochrome bo from Escherichia coli. Biochimica Et Biophysica Acta. 1141: 321-9. PMID 8382954 DOI: 10.1016/0005-2728(93)90060-S |
0.341 |
|
| 1993 |
Cheesman MR, Watmough NJ, Pires CA, Turner R, Brittain T, Gennis RB, Greenwood C, Thomson AJ. Cytochrome bo from Escherichia coli: identification of haem ligands and reaction of the reduced enzyme with carbon monoxide. The Biochemical Journal. 289: 709-18. PMID 8382047 DOI: 10.1042/Bj2890709 |
0.419 |
|
| 1993 |
Van Doren SR, Yun CH, Crofts AR, Gennis RB. Assembly of the Rieske iron-sulfur subunit of the cytochrome bc1 complex in the Escherichia coli and Rhodobacter sphaeroides membranes independent of the cytochrome b and c1 subunits. Biochemistry. 32: 628-36. PMID 8380704 DOI: 10.1021/Bi00053A031 |
0.335 |
|
| 1993 |
Krasnoselskaya I, Arutjunjan AM, Smirnova I, Gennis R, Konstantinov AA. Cyanide-reactive sites in cytochrome bd complex from E. coli. Febs Letters. 327: 279-83. PMID 8348954 DOI: 10.1016/0014-5793(93)81004-J |
0.382 |
|
| 1993 |
Calhoun MW, Lemieux LJ, Thomas JW, Hill JJ, Goswitz VC, Alben JO, Gennis RB. Spectroscopic characterization of mutants supports the assignment of histidine-419 as the axial ligand of heme o in the binuclear center of the cytochrome bo ubiquinol oxidase from Escherichia coli. Biochemistry. 32: 13254-61. PMID 8241181 DOI: 10.1021/Bi00211A038 |
0.436 |
|
| 1993 |
Sled' VD, Friedrich T, Leif H, Weiss H, Meinhardt SW, Fukumori Y, Calhoun MW, Gennis RB, Ohnishi T. Bacterial NADH-quinone oxidoreductases: Iron-sulfur clusters and related problems Journal of Bioenergetics and Biomembranes. 25: 347-356. PMID 8226716 DOI: 10.1007/Bf00762460 |
0.347 |
|
| 1993 |
Lemon DD, Calhoun MW, Gennis RB, Woodruff WH. The gateway to the active site of heme-copper oxidases. Biochemistry. 32: 11953-6. PMID 8218269 DOI: 10.1021/Bi00096A002 |
0.401 |
|
| 1993 |
Calhoun MW, Hill JJ, Lemieux LJ, Ingledew WJ, Alben JO, Gennis RB. Site-directed mutants of the cytochrome bo ubiquinol oxidase of Escherichia coli: amino acid substitutions for two histidines that are putative CuB ligands. Biochemistry. 32: 11524-9. PMID 8218219 DOI: 10.1021/bi00094a008 |
0.332 |
|
| 1993 |
Thomas JW, Lemieux LJ, Alben JO, Gennis RB. Site-directed mutagenesis of highly conserved residues in helix VIII of subunit I of the cytochrome bo ubiquinol oxidase from Escherichia coli: an amphipathic transmembrane helix that may be important in conveying protons to the binuclear center. Biochemistry. 32: 11173-80. PMID 8218180 DOI: 10.1021/Bi00092A029 |
0.445 |
|
| 1993 |
Jiang FS, Zuberi TM, Cornelius JB, Clarkson RB, Gennis RB, Belford RL. Nitrogen and proton ENDOR of cytochrome d, hemin, and metmyoglobin in frozen solutions Journal of the American Chemical Society. 115: 10286-10292. DOI: 10.1021/Ja00075A052 |
0.355 |
|
| 1993 |
Kahlow MA, Loehr TM, Zuberi TM, Gennis RB. The oxygenated complex of cytochrome d terminal oxidase: direct evidence for iron-oxygen coordination in a chlorin-containing enzyme by resonance Raman spectroscopy Journal of the American Chemical Society. 115: 5845-5846. DOI: 10.1021/Ja00066A071 |
0.349 |
|
| 1993 |
Wang J, Ching YC, Rousseau DL, Hill JJ, Rumbley J, Gennis RB. Similar carbon monoxide binding sites in bacterial cytochrome bo and mammalian cytochrome c oxidase Journal of the American Chemical Society. 115: 3390-3391. DOI: 10.1021/Ja00061A072 |
0.412 |
|
| 1993 |
Hosler J, Espe M, Fetter J, Shapleigh J, Thomas J, Tecklenburg M, Kim Y, Zhen Y, Gennis R, Babcock G, Ferguson-Miller S. Metal center ligation and proton pumping in cytochrome c oxidase Journal of Inorganic Biochemistry. 51: 275. DOI: 10.1016/0162-0134(93)85307-T |
0.337 |
|
| 1992 |
Newton G, Yun CH, Gennis RB. Analysis of the topology of the cytochrome d terminal oxidase complex of Escherichia coli by alkaline phosphatase fusions. Molecular Microbiology. 5: 2511-8. PMID 1724280 DOI: 10.1111/J.1365-2958.1991.Tb02097.X |
0.347 |
|
| 1992 |
Puustinen A, Morgan JE, Verkhovsky M, Thomas JW, Gennis RB, Wikström M. The low-spin heme site of cytochrome o from Escherichia coli is promiscuous with respect to heme type. Biochemistry. 31: 10363-9. PMID 1420155 DOI: 10.1021/Bi00157A026 |
0.4 |
|
| 1992 |
Calhoun MW, Gennis RB, Salerno JC. The formate complex of the cytochrome bo quinol oxidase of Escherichia coli exhibits a 'g = 12' EPR feature analogous to that of 'slow' cytochrome oxidase. Febs Letters. 309: 127-9. PMID 1324191 DOI: 10.1016/0014-5793(92)81079-2 |
0.384 |
|
| 1992 |
van der Oost J, Lappalainen P, Musacchio A, Warne A, Lemieux L, Rumbley J, Gennis RB, Aasa R, Pascher T, Malmström BG. Restoration of a lost metal-binding site: construction of two different copper sites into a subunit of the E. coli cytochrome o quinol oxidase complex. The Embo Journal. 11: 3209-17. PMID 1324168 DOI: 10.1002/J.1460-2075.1992.Tb05398.X |
0.444 |
|
| 1992 |
Shapleigh JP, Hosler JP, Tecklenburg MM, Kim Y, Babcock GT, Gennis RB, Ferguson-Miller S. Definition of the catalytic site of cytochrome c oxidase: specific ligands of heme a and the heme a3-CuB center. Proceedings of the National Academy of Sciences of the United States of America. 89: 4786-90. PMID 1317571 DOI: 10.1073/Pnas.89.11.4786 |
0.407 |
|
| 1992 |
Shapleigh JP, Gennis RB. Cloning, sequencing and deletion from the chromosome of the gene encoding subunit I of the aa3-type cytochrome c oxidase of Rhodobacter sphaeroides Molecular Microbiology. 6: 635-642. PMID 1313140 DOI: 10.1111/J.1365-2958.1992.Tb01511.X |
0.337 |
|
| 1992 |
Shapleigh JP, Hill JJ, Alben JO, Gennis RB. Spectroscopic and genetic evidence for two heme-Cu-containing oxidases in Rhodobacter sphaeroides Journal of Bacteriology. 174: 2338-2343. PMID 1313003 DOI: 10.1128/Jb.174.7.2338-2343.1992 |
0.403 |
|
| 1992 |
Gennis RB. Site-directed mutagenesis studies on subunit I of theaa3-type cytochrome c oxidase ofRhodobacter sphaeroides: a brief review of progress to date Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 1101: 184-187. DOI: 10.1016/0005-2728(92)90220-V |
0.345 |
|
| 1992 |
Semenov AY, Bloch DA, Crofts AR, Drachev LA, Gennis RB, Mulkidjanian AY, Yun C. Electrogenic events in chromatophores fromRhodobacter sphaeroides lacking high-potential cytochrome b of thebc1-complex Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 1101: 166-167. DOI: 10.1016/0005-2728(92)90203-E |
0.369 |
|
| 1992 |
Crofts A, Hacker B, Barquera B, Yun C, Gennis R. Structure and function of thebc-complex ofRhodobacter sphaeroides Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 1101: 162-165. DOI: 10.1016/0005-2728(92)90202-D |
0.339 |
|
| 1991 |
Pilkington SJ, Skehel JM, Gennis RB, Walker JE. Relationship between mitochondrial NADH-ubiquinone reductase and a bacterial NAD-reducing hydrogenase. Biochemistry. 30: 2166-75. PMID 1900194 DOI: 10.1021/Bi00222A021 |
0.355 |
|
| 1991 |
Newton G, Gennis RB. In vivo assembly of the cytochrome d terminal oxidase complex of Escherichia coli from genes encoding the two subunits expressed on separate plasmids. Biochimica Et Biophysica Acta. 1089: 8-12. PMID 1851043 DOI: 10.1016/0167-4781(91)90077-Y |
0.347 |
|
| 1991 |
Puustinen A, Finel M, Haltia T, Gennis RB, Wikström M. Properties of the two terminal oxidases of Escherichia coli. Biochemistry. 30: 3936-42. PMID 1850294 DOI: 10.1021/Bi00230A019 |
0.456 |
|
| 1991 |
Kahlow MA, Zuberi TM, Gennis RB, Loehr TM. Identification of a ferryl intermediate of Escherichia coli cytochrome d terminal oxidase by resonance Raman spectroscopy. Biochemistry. 30: 11485-9. PMID 1747367 DOI: 10.1021/Bi00113A001 |
0.393 |
|
| 1991 |
Dueweke TJ, Gennis RB. Proteolysis of the cytochrome d complex with trypsin and chymotrypsin localizes a quinol oxidase domain. Biochemistry. 30: 3401-6. PMID 1707310 DOI: 10.1021/Bi00228A007 |
0.422 |
|
| 1991 |
Oden KL, Gennis RB. Isolation and characterization of a new class of cytochrome d terminal oxidase mutants of Escherichia coli. Journal of Bacteriology. 173: 6174-83. PMID 1655701 DOI: 10.1128/Jb.173.19.6174-6183.1991 |
0.348 |
|
| 1991 |
Yun CH, Crofts AR, Gennis RB. Assignment of the histidine axial ligands to the cytochrome bH and cytochrome bL components of the bc1 complex from Rhodobacter sphaeroides by site-directed mutagenesis. Biochemistry. 30: 6747-54. PMID 1648391 DOI: 10.1021/Bi00241A017 |
0.385 |
|
| 1991 |
Cao J, Shapleigh J, Gennis R, Revzin A, Ferguson-Miller S. The gene encoding cytochrome c oxidase subunit II from Rhodobacter sphaeroides; comparison of the deduced amino acid sequence with sequences of corresponding peptides from other species Gene. 101: 133-137. PMID 1648008 DOI: 10.1016/0378-1119(91)90235-4 |
0.353 |
|
| 1991 |
Gennis RB. Some recent advances relating to prokaryotic cytochrome c reductases and cytochrome c oxidases. Biochimica Et Biophysica Acta. 1058: 21-4. PMID 1646011 DOI: 10.1016/S0005-2728(05)80260-9 |
0.412 |
|
| 1990 |
Miller MJ, Gennis RB. Purification and reconstitution of the cytochrome d terminal oxidase complex from Escherichia coli. Methods in Enzymology. 126: 87-94. PMID 2856143 DOI: 10.1016/S0076-6879(86)26011-5 |
0.399 |
|
| 1990 |
Azzi A, Gennis RB. Purification of the aa3-type cytochrome-c oxidase from Rhodopseudomonas sphaeroides. Methods in Enzymology. 126: 138-45. PMID 2856120 DOI: 10.1016/S0076-6879(86)26015-2 |
0.397 |
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| 1990 |
Runswick MJ, Gennis RB, Fearnley IM, Walker JE. Mitochondrial NADH:ubiquinone reductase: complementary DNA sequence of the import precursor of the bovine 75-kDa subunit. Biochemistry. 28: 9452-9. PMID 2514801 DOI: 10.1021/Bi00450A031 |
0.302 |
|
| 1990 |
Yun CH, Beci R, Crofts AR, Kaplan S, Gennis RB. Cloning and DNA sequencing of the fbc operon encoding the cytochrome bc1 complex from Rhodobacter sphaeroides. Characterization of fbc deletion mutants and complementation by a site-specific mutational variant. European Journal of Biochemistry / Febs. 194: 399-411. PMID 2176595 DOI: 10.1111/J.1432-1033.1990.Tb15633.X |
0.368 |
|
| 1990 |
Cotter PA, Chepuri V, Gennis RB, Gunsalus RP. Cytochrome o (cyoABCDE) and d (cydAB) oxidase gene expression in Escherichia coli is regulated by oxygen, pH and the fnr gene product Journal of Bacteriology. 172: 6333-6338. PMID 2172211 DOI: 10.1128/Jb.172.11.6333-6338.1990 |
0.355 |
|
| 1990 |
Chepuri V, Lemieux L, Hill J, Alben JO, Gennis RB. Recent studies of the cytochrome o terminal oxidase complex of Escherichia coli. Biochimica Et Biophysica Acta. 1018: 124-7. PMID 2168206 DOI: 10.1016/0005-2728(90)90231-R |
0.434 |
|
| 1990 |
Andrews KM, Crofts AR, Gennis RB. Large-scale purification and characterization of a highly active four-subunit cytochrome bc1 complex from Rhodobacter sphaeroides. Biochemistry. 29: 2645-51. PMID 2161250 DOI: 10.1021/Bi00463A004 |
0.387 |
|
| 1989 |
Saraste M, Raitio M, Jalli T, Chepuri V, Lemieux L, Gennis RB. Cytochrome o from Escherichia coli is structurally related to cytochrome aa3. Annals of the New York Academy of Sciences. 550: 314-24. PMID 2854403 DOI: 10.1111/J.1749-6632.1988.Tb35346.X |
0.33 |
|
| 1989 |
Meinhardt SW, Gennis RB, Ohnishi T. EPR studies of the cytochrome-d complex of Escherichia coli. Biochimica Et Biophysica Acta. 975: 175-84. PMID 2544229 DOI: 10.1016/S0005-2728(89)80216-6 |
0.313 |
|
| 1988 |
Georgiou CD, Cokic P, Carter K, Webster DA, Gennis RB. Relationships between membrane-bound cytochrome o from Vitreoscilla and that of Escherichia coli. Biochimica Et Biophysica Acta. 933: 179-83. PMID 3280028 DOI: 10.1016/0005-2728(88)90068-0 |
0.392 |
|
| 1988 |
Minghetti KC, Gennis RB. The two terminal oxidases of the aerobic respiratory chain of Escherichia coli each yield water and not peroxide as a final product. Biochemical and Biophysical Research Communications. 155: 243-8. PMID 2843179 DOI: 10.1016/S0006-291X(88)81075-1 |
0.394 |
|
| 1988 |
Georgiou CD, Dueweke TJ, Gennis RB. Regulation of expression of the cytochrome d terminal oxidase in Escherichia coli is transcriptional. Journal of Bacteriology. 170: 961-6. PMID 2828338 DOI: 10.1128/Jb.170.2.961-966.1988 |
0.327 |
|
| 1987 |
Au DC, Gennis RB. Cloning of the cyo locus encoding the cytochrome o terminal oxidase complex of Escherichia coli. Journal of Bacteriology. 169: 3237-42. PMID 3036778 DOI: 10.1128/Jb.169.7.3237-3242.1987 |
0.316 |
|
| 1987 |
Georgiou CD, Fang H, Gennis RB. Identification of the cydC locus required for expression of the functional form of the cytochrome d terminal oxidase complex in Escherichia coli Journal of Bacteriology. 169: 2107-2112. PMID 3032907 DOI: 10.1128/Jb.169.5.2107-2112.1987 |
0.324 |
|
| 1987 |
Gennis RB. The cytochromes ofEscherichia coli Fems Microbiology Letters. 46: 387-399. DOI: 10.1111/J.1574-6968.1987.Tb02475.X |
0.382 |
|
| 1987 |
Anraku Y, Gennis RB. The aerobic respiratory chain of Escherichia coli Trends in Biochemical Sciences. 12: 262-266. DOI: 10.1016/0968-0004(87)90131-9 |
0.414 |
|
| 1987 |
Livingston DJ, Shames SL, Gennis R, Walsh CT. Cyclopropylglyoxylate as a mechanistic probe of thiamine pyrophosphate dependent pyruvate-metabolizing enzymes Bioorganic Chemistry. 15: 358-365. DOI: 10.1016/0045-2068(87)90032-0 |
0.375 |
|
| 1986 |
Barassi CA, Kranz RG, Gennis RB. Characterization of monoclonal antibodies directed against pyruvate oxidase from Escherichia coli: Modulation of antibody-induced inhibition by enzyme conformation Biochemical and Biophysical Research Communications. 137: 884-891. PMID 3524564 DOI: 10.1016/0006-291X(86)91162-9 |
0.317 |
|
| 1985 |
Barassi CA, Kranz RG, Gennis RB. Succinate dehydrogenase in Rhodopseudomonas sphaeroides: Subunit composition and immunocross-reactivity with other related bacteria Journal of Bacteriology. 163: 778-782. PMID 3874866 DOI: 10.1128/Jb.163.2.778-782.1985 |
0.333 |
|
| 1985 |
Kranz RG, Gennis RB. Immunological investigation of the distribution of cytochromes related to the two terminal oxidases of Escherichia coli in other gram-negative bacteria Journal of Bacteriology. 161: 709-713. PMID 2981822 DOI: 10.1128/Jb.161.2.709-713.1985 |
0.36 |
|
| 1985 |
Au DC, Lorence RM, Gennis RB. Isolation and characterization of an Escherichia coli mutant lacking the cytochrome o terminal oxidase. Journal of Bacteriology. 161: 123-127. DOI: 10.1128/Jb.161.1.123-127.1985 |
0.338 |
|
| 1984 |
Lorence RM, Miller MJ, Borochov A, Faiman-Weinberg R, Gennis RB. Effects of pH and detergent on the kinetic and electrochemical properties of the purified cytochrome d terminal oxidase complex of Escherichia coli. Biochimica Et Biophysica Acta. 790: 148-53. PMID 6386051 DOI: 10.1016/0167-4838(84)90218-8 |
0.412 |
|
| 1984 |
Kranz RG, Barassi CA, Gennis RB. Immunological analysis of the heme proteins present in aerobically grown Escherichia coli Journal of Bacteriology. 158: 1191-1194. PMID 6373739 DOI: 10.1128/Jb.158.3.1191-1194.1984 |
0.357 |
|
| 1984 |
Koland JG, Miller MJ, Gennis RB. Reconstitution of the membrane-bound, ubiquinone-dependent pyruvate oxidase respiratory chain of Escherichia coli with the cytochrome d terminal oxidase. Biochemistry. 23: 445-53. PMID 6367818 DOI: 10.1021/Bi00298A008 |
0.399 |
|
| 1984 |
Lorence RM, Green GN, Gennis RB. Potentiometric analysis of the cytochromes of an Escherichia coli mutant strain lacking the cytochrome d terminal oxidase complex. Journal of Bacteriology. 157: 115-121. DOI: 10.1128/Jb.157.1.115-121.1984 |
0.387 |
|
| 1984 |
JONES RW, WEINER JH, GENNIS RB. Immunochemical analysis of membrane-bound antigens from Escherichia coli which have succinate dehydrogenase activity Biochemical Society Transactions. 12: 800-801. DOI: 10.1042/Bst0120800 |
0.304 |
|
| 1984 |
Koland JG, Miller MJ, Gennis RB. Potentiometric analysis of the purified cytochrome d terminal oxidase complex from Escherichia coli. Biochemistry. 23: 1051-1056. DOI: 10.1021/Bi00301A003 |
0.331 |
|
| 1983 |
Kranz RG, Barassi CA, Miller MJ, Green GN, Gennis RB. Immunological characterization of an Escherichia coli strain which is lacking cytochrome d Journal of Bacteriology. 156: 115-121. PMID 6311794 DOI: 10.1128/Jb.156.1.115-121.1983 |
0.314 |
|
| 1983 |
Matsushita K, Patel L, Gennis RB, Kaback HR. Reconstitution of active transport in proteoliposomes containing cytochrome o oxidase and lac carrier protein purified from Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America. 80: 4889-93. PMID 6308657 DOI: 10.1073/Pnas.80.16.4889 |
0.409 |
|
| 1983 |
Green GN, Gennis RB. Isolation and characterization of an Escherichia coli mutant lacking cytochrome d terminal oxidase. Journal of Bacteriology. 154: 1269-1275. DOI: 10.1128/Jb.154.3.1269-1275.1983 |
0.344 |
|
| 1982 |
Mather M, Blake R, Koland J, Schrock H, Russell P, O'Brien T, Hager LP, Gennis RB, O'Leary M. Escherichia coli pyruvate oxidase: interaction of a peripheral membrane protein with lipids. Biophysical Journal. 37: 87-8. PMID 19431517 DOI: 10.1016/S0006-3495(82)84613-4 |
0.387 |
|
| 1982 |
Jones RW, Kranz RG, Gennis RB. Immunochemical analysis of the membrane-bound succinate dehydrogenase of Escherichia coli Febs Letters. 142: 81-87. PMID 7049730 DOI: 10.1016/0014-5793(82)80224-X |
0.316 |
|
| 1982 |
Koland JG, O'Brien TA, Gennis RB. Role of arginine in the binding of thiamin pyrophosphate to Escherichia coli pyruvate oxidase. Biochemistry. 21: 2656-600. PMID 7046791 DOI: 10.1021/Bi00540A012 |
0.39 |
|
| 1982 |
O'Brien TA, Shelton E, Mather M, Gennis RB. Conformational studies of Escherichia coli pyruvate oxidase. Biochimica Et Biophysica Acta. 705: 321-9. PMID 6751398 DOI: 10.1016/0167-4838(82)90254-0 |
0.398 |
|
| 1982 |
Koland JG, Gennis RB. Proximity of reactive cysteine residue and flavin in Escherichia coli pyruvate oxidase as estimated by fluorescence energy transfer. Biochemistry. 21: 4438-42. PMID 6751388 DOI: 10.1021/Bi00261A038 |
0.329 |
|
| 1982 |
Gennis RB, Casey RP, Azzi A, Ludwig B. Purification and characterization of the cytochrome c oxidase from Rhodopseudomonas sphaeroides. European Journal of Biochemistry. 125: 189-95. PMID 6286309 DOI: 10.1111/J.1432-1033.1982.Tb06667.X |
0.422 |
|
| 1982 |
Kranz RG, Gennis RB. Isoelectric focusing and crossed immunoelectrophoresis of heme proteins in the Escherichia coli cytoplasmic membrane Journal of Bacteriology. 150: 36-45. PMID 6277868 DOI: 10.1128/Jb.150.1.36-45.1982 |
0.344 |
|
| 1981 |
Schrock HL, Gennis RB. The binding of a fluorescent activator 2-(N-decyl)aminonaphthalene-6-sulfonic acid to pyruvate oxidase. Biochimica Et Biophysica Acta. 615: 10-8. PMID 7000189 DOI: 10.1016/0005-2744(80)90003-0 |
0.387 |
|
| 1980 |
Mosberg HI, Scogin DA, Storm DR, Gennis RB. Proton nuclear magnetic resonance studies on bacitracin A and its interaction with zinc ion Biochemistry. 19: 3353-3357. PMID 7407048 DOI: 10.1021/Bi00555A039 |
0.333 |
|
| 1980 |
Schrock HL, Gennis RB. Specific ligand enhancement of the affinity of E. coli pyruvate oxidase for dipalmitoyl phosphatidylcholine. Biochimica Et Biophysica Acta. 614: 215-20. PMID 6994817 DOI: 10.1016/0005-2744(80)90182-5 |
0.398 |
|
| 1980 |
O'Brien TA, Kluger R, Pike DC, Gennis RB. Phosphonate analogues of pyruvate. Probes of substrate binding to pyruvate oxidase and other thiamin pyrophosphate-dependent decarboxylases. Biochimica Et Biophysica Acta. 613: 10-7. PMID 6990987 DOI: 10.1016/0005-2744(80)90186-2 |
0.38 |
|
| 1979 |
Shaw-Goldstein LA, Gennis RB, Walsh C. Identification, localization, and function of the thiamin pyrophosphate and flavin adenine dinucleotide dependent pyruvate oxidase in isolated membrane vesicles of Escherichia coli B. Biochemistry. 17: 5605-13. PMID 365232 DOI: 10.1021/Bi00619A004 |
0.304 |
|
| 1977 |
O'Brien TA, Schrock HL, Russell P, Blake R, Gennis RB. Preparation of Escherichia coli pyruvate oxidase utilizing a thiamine pyrophosphate affinity column. Biochimica Et Biophysica Acta. 452: 13-29. PMID 791368 DOI: 10.1016/0005-2744(76)90054-1 |
0.349 |
|
| 1977 |
O'Brien TA, Blake R, Gennis RB. Regulation by lipids of cofactor binding to a peripheral membrane enzyme: binding of thiamin pyrophosphate to pyruvate oxidase. Biochemistry. 16: 3105-9. PMID 329866 DOI: 10.1021/Bi00633A010 |
0.303 |
|
| 1977 |
Nieva-Gomez D, Gennis RB. Affinity of intact Escherichia coli for hydrophobic membrane probes is a function of the physiological state of the cells. Proceedings of the National Academy of Sciences of the United States of America. 74: 1811-5. PMID 325554 DOI: 10.1073/Pnas.74.5.1811 |
0.306 |
|
| 1977 |
Raj T, Russell P, Flygare WH, Gennis RB. Quasi-elastic light scattering studies on pyruvate oxidase. Biochimica Et Biophysica Acta. 481: 42-9. PMID 321031 DOI: 10.1016/0005-2744(77)90135-8 |
0.312 |
|
| 1976 |
Gennis RB, Strominger JL. Activation of C55-isoprenoid alcohol phosphokinase from Staphylococcus aureus. III. Activation by detergents. The Journal of Biological Chemistry. 251: 1277-82. PMID 176147 |
0.357 |
|
| 1976 |
Gennis RB, Sinensky M, Strominger JL. Activation of C55-isoprenoid alcohol phosphokinase from Staphylococcus aureus. II. Biophysical studies. The Journal of Biological Chemistry. 251: 1270-6. PMID 176146 |
0.4 |
|
| 1976 |
Gennis RB, Strominger JL. Activation of C55-isoprenoid alcohol phosphokinase from Staphylococcus aureus. I. Activation by phospholipids and fatty acids. The Journal of Biological Chemistry. 251: 1264-9. PMID 176145 |
0.337 |
|
| 1972 |
Gennis RB, Cantor CR. Use of nonspecific dye labeling for singlet energy-transfer measurements in complex systems. A simple model. Biochemistry. 11: 2509-17. PMID 5040656 DOI: 10.1021/Bi00763A020 |
0.464 |
|
| 1972 |
Gennis LS, Gennis RB, Cantor CR. Singlet energy-transfer studies on associating protein systems. Distance measurements on trypsin, -chymotrypsin, and their protein inhibitors. Biochemistry. 11: 2517-24. PMID 4339245 DOI: 10.1021/Bi00763A021 |
0.47 |
|
| 1972 |
Gennis RB, Cantor CR. Optical studies of a conformational change in DNA before melting. Journal of Molecular Biology. 65: 381-99. PMID 4336863 DOI: 10.1016/0022-2836(72)90196-9 |
0.394 |
|
| 1970 |
Gennis RB, Cantor CR. Optical properties of specific complexes between complementary oligoribonucleotides. Biochemistry. 9: 4714-25. PMID 5482270 DOI: 10.1021/Bi00826A014 |
0.431 |
|
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