Year |
Citation |
Score |
2019 |
Szundi I, Funatogawa C, Soulimane T, Einarsdóttir Ó. The Reactions of O and NO with Mixed-Valence ba Cytochrome c Oxidase from Thermus thermophilus. Biophysical Journal. PMID 31870538 DOI: 10.1016/J.Bpj.2019.11.3390 |
0.799 |
|
2016 |
Funatogawa C, Li Y, Chen Y, McDonald W, Szundi I, Fee JA, Stout CD, Einarsdóttir Ó. Role of the Conserved Valine 236 in Access of Ligands to the Active Site of Thermus thermophilus ba3 Cytochrome Oxidase. Biochemistry. PMID 28026953 DOI: 10.1021/Acs.Biochem.6B00590 |
0.807 |
|
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 |
0.444 |
|
2015 |
Einarsdóttir O, McDonald W, Funatogawa C, Szundi I, Woodruff WH, Dyer RB. The pathway of O₂to the active site in heme-copper oxidases. Biochimica Et Biophysica Acta. 1847: 109-18. PMID 24998308 DOI: 10.1016/J.Bbabio.2014.06.008 |
0.786 |
|
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 |
0.733 |
|
2014 |
McDonald W, Funatogawa C, Li Y, Chen Y, Szundi I, Fee JA, Stout CD, Einarsdóttir O. Conserved glycine 232 in the ligand channel of ba3 cytochrome oxidase from Thermus thermophilus. Biochemistry. 53: 4467-75. PMID 24937405 DOI: 10.1021/Bi500289H |
0.812 |
|
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 |
0.548 |
|
2014 |
Funatogawa C, Li Y, Chen Y, Szundi I, Fee JA, Stout CD, Einarsdottir O. The Roles of the Highly Conserved Amino Acid Residues Val236 and Gly232 in the Ligand Channel of Ba3 Cytochrome C Oxidase from Thermus Thermophilus Biophysical Journal. 106: 587a. DOI: 10.1016/J.Bpj.2013.11.3253 |
0.784 |
|
2013 |
Silva BA, Einarsdóttir O, Fink AL, Uversky VN. Biophysical Characterization of α-Synuclein and Rotenone Interaction. Biomolecules. 3: 703-32. PMID 24970188 DOI: 10.3390/biom3030703 |
0.586 |
|
2013 |
McDonald W, Funatogawa C, Li Y, Szundi I, Chen Y, Fee JA, Stout CD, Einarsdóttir Ó. Ligand access to the active site in Thermus thermophilus ba(3) and bovine heart aa(3) cytochrome oxidases. Biochemistry. 52: 640-52. PMID 23282175 DOI: 10.1021/Bi301358A |
0.8 |
|
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 |
0.802 |
|
2012 |
Einarsdóttir O, Funatogawa C, Soulimane T, Szundi I. Kinetic studies of the reactions of O(2) and NO with reduced Thermus thermophilus ba(3) and bovine aa(3) using photolabile carriers. Biochimica Et Biophysica Acta. 1817: 672-9. PMID 22201543 DOI: 10.1016/J.Bbabio.2011.12.005 |
0.82 |
|
2010 |
Szundi I, Funatogawa C, Fee JA, Soulimane T, Einarsdóttir O. CO impedes superfast O2 binding in ba3 cytochrome oxidase from Thermus thermophilus. Proceedings of the National Academy of Sciences of the United States of America. 107: 21010-5. PMID 21097703 DOI: 10.1073/Pnas.1008603107 |
0.811 |
|
2010 |
McDonald WJ, Einarsdóttir O. Solvent effects on the physicochemical properties of the cross-linked histidine-tyrosine ligand of cytochrome c oxidase. The Journal of Physical Chemistry. B. 114: 6409-25. PMID 20415431 DOI: 10.1021/Jp909574V |
0.429 |
|
2009 |
Mahoney ME, Oliver A, Einarsdóttir Ó, Konopelski JP. Synthesis of a cyclic pentapeptide mimic of the active site His-Tyr cofactor of cytochrome c oxidase Journal of Organic Chemistry. 74: 8212-8218. PMID 19810693 DOI: 10.1021/Jo901744Y |
0.336 |
|
2008 |
McDonald WJ, Einarsdóttir O. Solvent effects on the vibrational frequencies of the phenolate anion, the para-cresolate anion, and their radicals. The Journal of Physical Chemistry. A. 112: 11400-13. PMID 18939813 DOI: 10.1021/Jp800169W |
0.304 |
|
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 |
0.625 |
|
2007 |
White KN, Sen I, Szundi I, Landaverry YR, Bria LE, Konopelski JP, Olmstead MM, Einarsdóttir Ó. Synthesis and structural characterization of cross-linked histidine-phenol Cu(II) complexes as cytochrome c oxidase active site models Chemical Communications. 3252-3254. PMID 17668091 DOI: 10.1039/B703835F |
0.358 |
|
2006 |
Szundi I, Rose MJ, Sen I, Eroy-Reveles AA, Mascharak PK, Einarsdóttir O. A new approach for studying fast biological reactions involving nitric oxide: Generation of NO using photolabile ruthenium and manganese NO donors Photochemistry and Photobiology. 82: 1377-1384. PMID 17421079 DOI: 10.1562/2006-07-25-Rc-984 |
0.426 |
|
2006 |
Winterle JS, Einarsdóttir O. Photoreactions of cytochrome C oxidase. Photochemistry and Photobiology. 82: 711-9. PMID 16789843 DOI: 10.1562/2005-09-14-Ra-684 |
0.399 |
|
2006 |
Konopelski JP, Landaverry YR, White KN, Olmstead MM, Einarsdóttir Ó. Cytochrome C oxidase active site mimics : New ligands for copper and an unexpected oxidative C-C bond formation Heterocycles. 70: 147-152. DOI: 10.3987/Com-06-S(W)46 |
0.399 |
|
2004 |
Szundi I, Cappuccio J, Einarsdóttir O. Amplitude analysis of single-wavelength time-dependent absorption data does not support the conventional sequential mechanism for the reduction of dioxygen to water catalyzed by bovine heart cytochrome c oxidase. Biochemistry. 43: 15746-58. PMID 15595830 DOI: 10.1021/Bi049408P |
0.788 |
|
2004 |
Einarsdóttir O, Szundi I. Time-resolved optical absorption studies of cytochrome oxidase dynamics. Biochimica Et Biophysica Acta. 1655: 263-73. PMID 15100041 DOI: 10.1016/J.Bbabio.2003.07.011 |
0.493 |
|
2003 |
Szundi I, Van Eps N, Einarsdóttir O. pH dependence of the reduction of dioxygen to water by cytochrome c oxidase. 2. Branched electron transfer pathways linked by proton transfer. Biochemistry. 42: 5074-90. PMID 12718551 DOI: 10.1021/Bi020483E |
0.752 |
|
2003 |
Van Eps N, Szundi I, Einarsdóttir O. pH dependence of the reduction of dioxygen to water by cytochrome c oxidase. 1. The P(R) state is a pH-dependent mixture of three intermediates, A, P, and F. Biochemistry. 42: 5065-73. PMID 12718550 DOI: 10.1021/Bi020482M |
0.733 |
|
2002 |
Einarsdóttir O, Szundi I, Van Eps N, Sucheta A. P(M) and P(R) forms of cytochrome c oxidase have different spectral properties. Journal of Inorganic Biochemistry. 91: 87-93. PMID 12121765 DOI: 10.1016/S0162-0134(02)00377-X |
0.772 |
|
2001 |
Szundi I, Cappuccio JA, Borovok N, Kotlyar aAB, Einarsdóttir Ó. Photoinduced electron transfer in the cytochrome c/cytochrome c oxidase complex using thiouredopyrenetrisulfonate-labeled cytochrome c. Optical multichannel detection. Biochemistry. 40: 2186-2193. PMID 11329287 DOI: 10.1021/Bi002341V |
0.772 |
|
2001 |
Szundi I, Liao G, Einarsdóttir Ó. Near-infrared time-resolved optical absorption studies of the reaction of fully reduced cytochrome c oxidase with dioxygen. Biochemistry. 40: 2332-2339. PMID 11327853 DOI: 10.1021/Bi002220V |
0.463 |
|
2000 |
Eps NV, Szundi aI, Einarsdóttir Ó. A new approach for studying fast biological reactions involving dioxygen: the reaction of fully reduced cytochrome c oxidase with O2. Biochemistry. 39: 14576-14582. PMID 11087413 DOI: 10.1021/Bi000955U |
0.446 |
|
2000 |
Kotlyar A, Borovok N, Hazani M, Szundi I, Einarsdóttir Ó. Photoinduced intracomplex electron transfer between cytochrome c oxidase and TUPS‐modified cytochrome c Febs Journal. 267: 5805-5809. PMID 10971592 DOI: 10.1046/J.1432-1327.2000.01655.X |
0.392 |
|
2000 |
Farver O, Einarsdóttir Ó, Pecht I. Electron transfer rates and equilibrium within cytochrome c oxidase. Febs Journal. 267: 950-954. PMID 10672001 DOI: 10.1046/J.1432-1327.2000.01072.X |
0.435 |
|
1999 |
Paula S, Sucheta A, Szundi I, Einarsdóttir Ó. Proton and electron transfer during the reduction of molecular oxygen by fully reduced cytochrome c oxidase: a flow-flash investigation using optical multichannel detection. Biochemistry. 38: 3025-3033. PMID 10074355 DOI: 10.1021/Bi981351H |
0.448 |
|
1999 |
Howe L, Sucheta A, Einarsdóttir Ó, Zhang JZ. Time-resolved studies of the excited-state dynamics of meso-tetra(hydroxylphenyl)chlorin in solution. Photochemistry and Photobiology. 69: 617-623. DOI: 10.1111/J.1751-1097.1999.Tb03337.X |
0.339 |
|
1998 |
Sucheta A, Szundi I, Einarsdóttir Ó. Intermediates in the reaction of fully reduced cytochrome c oxidase with dioxygen. Biochemistry. 37: 17905-17914. PMID 9922158 DOI: 10.1021/Bi981092W |
0.429 |
|
1997 |
Sucheta A, Georgiadis KE, Einarsdóttir Ó. Mechanism of cytochrome c oxidase-catalyzed reduction of dioxygen to water: evidence for peroxy and ferryl intermediates at room temperature. Biochemistry. 36: 554-565. PMID 9012671 DOI: 10.1021/Bi962422K |
0.426 |
|
1995 |
Einarsdóttir Ó. Fast reactions of cytochrome oxidase. Biochimica Et Biophysica Acta. 1229: 129-147. PMID 7727494 DOI: 10.1016/0005-2728(94)00196-C |
0.356 |
|
1995 |
MacArthur R, Sucheta A, Chong FFS, Einarsdottir O. Photodissociation of a (mu-peroxo)(mu-hydroxo)bis[bis(bipyridyl)-cobalt(III)] complex: a tool to study fast biological reactions involving O2 Proceedings of the National Academy of Sciences of the United States of America. 92: 8105-8109. PMID 7667252 DOI: 10.1073/Pnas.92.18.8105 |
0.441 |
|
1994 |
Georgiadis KE, Jhon N, Einarsdottir O. Time-resolved Optical Absorption Studies of Intramolecular Electron Transfer in Cytochrome C Oxidase Biochemistry. 33: 9245-9256. PMID 8049226 DOI: 10.1021/Bi00197A028 |
0.452 |
|
1994 |
Georgiadis K, Jhon N, Einarsdottir O. Corrections - Time-Resolved Optical Absorption Studies of Intramolecular Electron Transfer in Cytochrome c Oxidase Biochemistry. 33: 12936-12936. DOI: 10.1021/Bi00209A600 |
0.381 |
|
1993 |
Georgiadis K, Einarsdóttir Ó. The reaction of cytochrome c oxidase with O2 probed by flow-flash transient multichannel absorption spectroscopy Journal of Inorganic Biochemistry. 51: 305. DOI: 10.1016/0162-0134(93)85337-8 |
0.47 |
|
1992 |
Goldbeck RA, Einarsdóttir O, Dawes TD, O'Connor DB, Surerus KK, Fee JA, Kliger DS. Magnetic circular dichroism study of cytochrome ba3 from Thermus thermophilus: spectral contributions from cytochromes b and a3 and nanosecond spectroscopy of CO photodissociation intermediates. Biochemistry. 31: 9376-87. PMID 1327113 DOI: 10.1021/Bi00154A008 |
0.42 |
|
1992 |
Einarsdottir O, Dawes TD, Georgiadis KE. New Transients in the Electron-Transfer Dynamics of Photolyzed Mixed- Valence CO-Cytochrome c Oxidase Proceedings of the National Academy of Sciences of the United States of America. 89: 6934-6937. PMID 1323122 DOI: 10.1073/Pnas.89.15.6934 |
0.417 |
|
1992 |
Einarsdóttir O, Georgiadis KE, Dawes TD. Evidence for a band III analogue in the near-infrared absorption spectra of cytochrome c oxidase. Biochemical and Biophysical Research Communications. 184: 1035-1041. PMID 1315522 DOI: 10.1016/0006-291X(92)90695-H |
0.379 |
|
1991 |
Goldbeck RA, Dawes TD, Einarsdóttir O, Woodruff WH, Kliger DS. Time-resolved magnetic circular dichroism spectroscopy of photolyzed carbonmonoxy cytochrome c oxidase (cytochrome aa3). Biophysical Journal. 60: 125-34. PMID 1653049 DOI: 10.1016/S0006-3495(91)82036-7 |
0.445 |
|
1991 |
K. Surerus K, Oertling W, Fan C, Einarsdóttir Ó, Dyer R, Antholine WE, Hoffman BM, Woodruff WH, Fee JA. Spectroscopic characterization of the Fe(II)a·CN complex of Thermus thermophilus cytochrome ba3: A novel reaction of a terminal oxidase with cyanide Journal of Inorganic Biochemistry. 43: 352. DOI: 10.1016/0162-0134(91)84339-B |
0.328 |
|
1991 |
Woodruff WH, Dyer R, Peterson K, Stoutland P, Bagley K, Einarsdóttir Ó, Kliger DS, Goldbeck R, Dawes T, Martin J, Lambry J, Palmer G, Atherton SJ, Hubig SM. Ultrafast and not-so-fast dynamics of cytochrome oxidase: The ligand shuttle and its possible relevance to proton translocation Journal of Inorganic Biochemistry. 43: 351. DOI: 10.1016/0162-0134(91)84338-A |
0.34 |
|
1989 |
Dyer RB, Einarsdottir O, Killough PM, Lopez-Garriga JJ, Woodruff WH. Transient binding of photodissociated carbon monoxide to CuB+ of eukaryotic cytochrome oxidase at ambient temperature. Direct evidence from time-resolved infrared spectroscopy Journal of the American Chemical Society. 111: 7657-7659. DOI: 10.1021/Ja00201A080 |
0.362 |
|
1988 |
Einarsdottir O, Choc MG, Weldon S, Caughey WS. The site and mechanism of dioxygen reduction in bovine heart cytochrome c oxidase Journal of Biological Chemistry. 263: 13641-13654. PMID 2843526 |
0.646 |
|
1988 |
Einarsdottir O, Caughey WS. Interactions of the anesthetic nitrous oxide with bovine heart cytochrome c oxidase. Effects on protein structure, oxidase activity, and other properties Journal of Biological Chemistry. 263: 9199-9205. PMID 2837481 |
0.652 |
|
1985 |
Einarsdóttir O, Caughey WS. Bovine heart cytochrome c oxidase preparations contain high affinity binding sites for magnesium as well as for zinc, copper, and heme iron Biochemical and Biophysical Research Communications. 129: 840-847. PMID 2990471 DOI: 10.1016/0006-291X(85)91968-0 |
0.541 |
|
1984 |
Einarsdóttir O, Caughey WS. Zinc is a constituent of bovine heart cytochrome c oxidase preparations Biochemical and Biophysical Research Communications. 124: 836-842. PMID 6095824 DOI: 10.1016/0006-291X(84)91033-7 |
0.526 |
|
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