| Year |
Citation |
Score |
| 2015 |
Takayama SJ, Loutet SA, Mauk AG, Murphy ME. A Ferric-Peroxo Intermediate in the Oxidation of Heme by IsdI. Biochemistry. 54: 2613-21. PMID 25853501 DOI: 10.1021/Acs.Biochem.5B00239 |
0.365 |
|
| 2014 |
Saer RG, Pan J, Hardjasa A, Lin S, Rosell F, Mauk AG, Woodbury NW, Murphy ME, Beatty JT. Structural and kinetic properties of Rhodobacter sphaeroides photosynthetic reaction centers containing exclusively Zn-coordinated bacteriochlorophyll as bacteriochlorin cofactors. Biochimica Et Biophysica Acta. 1837: 366-74. PMID 24316146 DOI: 10.1016/J.Bbabio.2013.11.015 |
0.353 |
|
| 2012 |
Alam S, Yee J, Couture M, Takayama SJ, Tseng WH, Mauk AG, Rafferty S. Cytochrome b5 from Giardia lamblia. Metallomics : Integrated Biometal Science. 4: 1255-61. PMID 23151674 DOI: 10.1039/C2Mt20152F |
0.39 |
|
| 2012 |
Kuo HH, Mauk AG. Indole peroxygenase activity of indoleamine 2,3-dioxygenase. Proceedings of the National Academy of Sciences of the United States of America. 109: 13966-71. PMID 22891315 DOI: 10.1073/Pnas.1207191109 |
0.32 |
|
| 2012 |
Ukpabi G, Takayama SJ, Mauk AG, Murphy ME. Inactivation of the heme degrading enzyme IsdI by an active site substitution that diminishes heme ruffling. The Journal of Biological Chemistry. 287: 34179-88. PMID 22891243 DOI: 10.1074/Jbc.M112.393249 |
0.341 |
|
| 2012 |
Wong SG, Abdulqadir R, Le Brun NE, Moore GR, Mauk AG. Fe-haem bound to Escherichia coli bacterioferritin accelerates iron core formation by an electron transfer mechanism. The Biochemical Journal. 444: 553-60. PMID 22458666 DOI: 10.1042/Bj20112200 |
0.324 |
|
| 2012 |
Kumar R, Mauk AG. Protonation and anion binding control the kinetics of iron release from human transferrin. The Journal of Physical Chemistry. B. 116: 3795-807. PMID 22364386 DOI: 10.1021/Jp205879H |
0.359 |
|
| 2011 |
Takayama SJ, Ukpabi G, Murphy ME, Mauk AG. Electronic properties of the highly ruffled heme bound to the heme degrading enzyme IsdI. Proceedings of the National Academy of Sciences of the United States of America. 108: 13071-6. PMID 21788475 DOI: 10.1073/Pnas.1101459108 |
0.378 |
|
| 2011 |
Rosell FI, Kuo HH, Mauk AG. NADH oxidase activity of indoleamine 2,3-dioxygenase. The Journal of Biological Chemistry. 286: 29273-83. PMID 21690092 DOI: 10.1074/Jbc.M111.262139 |
0.314 |
|
| 2011 |
Rosell FI, Mauk AG. Photochemical reagents for the study of metalloproteins by flash photolysis Coordination Chemistry Reviews. 255: 737-756. DOI: 10.1016/J.Ccr.2010.11.025 |
0.331 |
|
| 2010 |
Mauk MR, Mauk AG. Metal ions and electrolytes regulate the dissociation of heme from human hemopexin at physiological pH. The Journal of Biological Chemistry. 285: 20499-506. PMID 20430887 DOI: 10.1074/Jbc.M110.123406 |
0.351 |
|
| 2009 |
Mauk MR, Rosell FI, Mauk AG. Metal ion facilitated dissociation of heme from b-type heme proteins. Journal of the American Chemical Society. 131: 16976-83. PMID 19874033 DOI: 10.1021/Ja907484J |
0.396 |
|
| 2009 |
Kumar R, Mauk AG. Atypical effects of salts on the stability and iron release kinetics of human transferrin. The Journal of Physical Chemistry. B. 113: 12400-9. PMID 19685917 DOI: 10.1021/Jp903257C |
0.305 |
|
| 2009 |
Carr G, Tay W, Bottriell H, Andersen SK, Mauk AG, Andersen RJ. Plectosphaeroic acids A, B, and C, indoleamine 2,3-dioxygenase inhibitors produced in culture by a marine isolate of the fungus Plectosphaerella cucumerina. Organic Letters. 11: 2996-9. PMID 19537768 DOI: 10.1021/Ol900972J |
0.303 |
|
| 2009 |
Lin S, Jaschke PR, Wang H, Paddock M, Tufts A, Allen JP, Rosell FI, Mauk AG, Woodbury NW, Beatty JT. Electron transfer in the Rhodobacter sphaeroides reaction center assembled with zinc bacteriochlorophyll. Proceedings of the National Academy of Sciences of the United States of America. 106: 8537-42. PMID 19439660 DOI: 10.1073/Pnas.0812719106 |
0.368 |
|
| 2009 |
Wong SG, Tom-Yew SA, Lewin A, Le Brun NE, Moore GR, Murphy ME, Mauk AG. Structural and mechanistic studies of a stabilized subunit dimer variant of Escherichia coli bacterioferritin identify residues required for core formation. The Journal of Biological Chemistry. 284: 18873-81. PMID 19439409 DOI: 10.1074/Jbc.M901747200 |
0.35 |
|
| 2008 |
Basova LV, Tiktopulo EI, Kutyshenko VP, Mauk AG, Bychkova VE. Phospholipid membranes affect tertiary structure of the soluble cytochrome b5 heme-binding domain. Biochimica Et Biophysica Acta. 1778: 1015-26. PMID 18275841 DOI: 10.1016/J.Bbamem.2007.12.028 |
0.362 |
|
| 2008 |
Ludwiczek S, Rosell FI, Ludwiczek ML, Mauk AG. Recombinant expression and initial characterization of the putative human enteric ferric reductase Dcytb. Biochemistry. 47: 753-61. PMID 18092813 DOI: 10.1021/Bi701793A |
0.382 |
|
| 2007 |
Wang ZH, Lin YW, Rosell FI, Ni FY, Lu HJ, Yang PY, Tan XS, Li XY, Huang ZX, Mauk AG. Converting cytochrome C into a peroxidase-like metalloenzyme by molecular design. Chembiochem : a European Journal of Chemical Biology. 8: 607-9. PMID 17328023 DOI: 10.1002/Cbic.200600547 |
0.32 |
|
| 2006 |
Lim AR, Sishta BP, Mauk AG. Contribution of the heme propionate groups to the electron transfer and electrostatic properties of myoglobin. Journal of Inorganic Biochemistry. 100: 2017-23. PMID 17070916 DOI: 10.1016/J.Jinorgbio.2006.08.019 |
0.401 |
|
| 2006 |
Pereira A, Vottero E, Roberge M, Mauk AG, Andersen RJ. Indoleamine 2,3-dioxygenase inhibitors from the Northeastern Pacific Marine Hydroid Garveia annulata. Journal of Natural Products. 69: 1496-9. PMID 17067170 DOI: 10.1021/Np060111X |
0.309 |
|
| 2006 |
Bai E, Rosell FI, Lige B, Mauk MR, Lelj-Garolla B, Moore GR, Mauk AG. Functional characterization of the dimerization domain of the ferric uptake regulator (Fur) of Pseudomonas aeruginosa. The Biochemical Journal. 400: 385-92. PMID 16928194 DOI: 10.1042/Bj20061168 |
0.319 |
|
| 2004 |
Liang ZX, Kurnikov IV, Nocek JM, Mauk AG, Beratan DN, Hoffman BM. Dynamic docking and electron-transfer between cytochrome b5 and a suite of myoglobin surface-charge mutants. Introduction of a functional-docking algorithm for protein-protein complexes. Journal of the American Chemical Society. 126: 2785-98. PMID 14995196 DOI: 10.1021/Ja038163L |
0.393 |
|
| 2003 |
Assfalg M, Bertini I, Turano P, Mauk AG, Winkler JR, Gray HB. 15N-1H Residual dipolar coupling analysis of native and alkaline-K79A Saccharomyces cerevisiae cytochrome c. Biophysical Journal. 84: 3917-23. PMID 12770897 DOI: 10.1016/S0006-3495(03)75119-4 |
0.608 |
|
| 2003 |
Assfalg M, Bertini I, Dolfi A, Turano P, Mauk AG, Rosell FI, Gray HB. Structural model for an alkaline form of ferricytochrome C. Journal of the American Chemical Society. 125: 2913-22. PMID 12617658 DOI: 10.1021/Ja027180S |
0.431 |
|
| 2003 |
Villegas JA, Rosell FI, Mauk AG. Cytochrome c without tryptophan: The W59A variant Journal of Inorganic Biochemistry. 96: 244. DOI: 10.1016/S0162-0134(03)80794-8 |
0.372 |
|
| 2002 |
Zhang H, He S, Mauk AG. Radical formation at Tyr39 and Tyr153 following reaction of yeast cytochrome c peroxidase with hydrogen peroxide. Biochemistry. 41: 13507-13. PMID 12427011 DOI: 10.1021/Bi026122G |
0.381 |
|
| 2002 |
Rosell FI, Mauk AG. Spectroscopic properties of a mitochondrial cytochrome C with a single thioether bond to the heme prosthetic group. Biochemistry. 41: 7811-8. PMID 12056913 DOI: 10.1021/Bi016060E |
0.392 |
|
| 2002 |
Brown MA, Stenberg LM, Mauk AG. Identification of catalytically important amino acids in human ceruloplasmin by site-directed mutagenesis. Febs Letters. 520: 8-12. PMID 12044861 DOI: 10.1016/S0014-5793(02)02652-2 |
0.323 |
|
| 2001 |
Witting PK, Mauk AG, Douglas DJ, Stocker R. Reaction of human myoglobin and peroxynitrite: characterizing biomarkers for myoglobin-derived oxidative stress. Biochemical and Biophysical Research Communications. 286: 352-6. PMID 11500044 DOI: 10.1006/Bbrc.2001.5397 |
0.333 |
|
| 2001 |
Witting PK, Mauk AG. Reaction of human myoglobin and H2O2. Electron transfer between tyrosine 103 phenoxyl radical and cysteine 110 yields a protein-thiyl radical. The Journal of Biological Chemistry. 276: 16540-7. PMID 11278969 DOI: 10.1074/Jbc.M011707200 |
0.303 |
|
| 2001 |
Couture MM, Colbert CL, Babini E, Rosell FI, Mauk AG, Bolin JT, Eltis LD. Characterization of BphF, a Rieske-type ferredoxin with a low reduction potential. Biochemistry. 40: 84-92. PMID 11141059 DOI: 10.1021/Bi001780R |
0.559 |
|
| 2001 |
Witting PK, Douglas DJ, Mauk AG. Reaction of human myoglobin and nitric oxide. Heme iron or protein sulfhydryl (s) nitrosation dependence on the absence or presence of oxygen. The Journal of Biological Chemistry. 276: 3991-8. PMID 11053410 DOI: 10.1074/Jbc.M005758200 |
0.36 |
|
| 2000 |
Silchenko S, Sippel ML, Kuchment O, Benson DR, Mauk AG, Altuve A, Rivera M. Hemin is kinetically trapped in cytochrome b(5) from rat outer mitochondrial membrane. Biochemical and Biophysical Research Communications. 273: 467-72. PMID 10873629 DOI: 10.1006/Bbrc.2000.2968 |
0.372 |
|
| 2000 |
Villegas JA, Mauk AG, Vazquez-Duhalt R. A cytochrome c variant resistant to heme degradation by hydrogen peroxide. Chemistry & Biology. 7: 237-44. PMID 10780923 DOI: 10.1016/S1074-5521(00)00098-3 |
0.373 |
|
| 2000 |
Ness SR, Lo TP, Mauk AG. Structural models for the alkaline conformers of yeastiso-1-ferricytochromec Israel Journal of Chemistry. 40: 21-25. DOI: 10.1560/Pk7U-Lepj-Etb5-997X |
0.36 |
|
| 1999 |
Couture MM, Auger M, Rosell F, Mauk AG, Boubour E, Lennox RB, Eltis LD. Investigation of the role of a surface patch in the self-association of Chromatium vinosum high potential iron-sulfur protein. Biochimica Et Biophysica Acta. 1433: 159-69. PMID 10446369 DOI: 10.1016/S0167-4838(99)00137-5 |
0.591 |
|
| 1999 |
Döpner S, Hildebrandt P, Rosell FI, Mauk AG, von Walter M, Buse G, Soulimane T. The structural and functional role of lysine residues in the binding domain of cytochrome c in the electron transfer to cytochrome c oxidase. European Journal of Biochemistry / Febs. 261: 379-91. PMID 10215847 DOI: 10.1046/J.1432-1327.1999.00249.X |
0.485 |
|
| 1998 |
Johnson MB, Adamson JG, Mauk AG. Functional comparison of specifically cross-linked hemoglobins biased toward the R and T states. Biophysical Journal. 75: 3078-84. PMID 9826627 DOI: 10.1016/S0006-3495(98)77748-3 |
0.332 |
|
| 1998 |
Wan L, Twitchett MB, Eltis LD, Mauk AG, Smith M. In vitro evolution of horse heart myoglobin to increase peroxidase activity Proceedings of the National Academy of Sciences of the United States of America. 95: 12825-12831. PMID 9788999 DOI: 10.1073/Pnas.95.22.12825 |
0.47 |
|
| 1998 |
Hildebrand DP, Lim KT, Rosell FI, Twitchett MB, Wan L, Mauk AG. Spectroscopic and functional studies of a novel quadruple myoglobin variant with increased peroxidase activity Journal of Inorganic Biochemistry. 70: 11-16. PMID 9661283 DOI: 10.1016/S0162-0134(98)00007-5 |
0.378 |
|
| 1998 |
Moore GR, Cox MC, Crowe D, Osborne MJ, Rosell FI, Bujons J, Barker PD, Mauk MR, Mauk AG. N epsilon,N epsilon-dimethyl-lysine cytochrome c as an NMR probe for lysine involvement in protein-protein complex formation. The Biochemical Journal. 332: 439-49. PMID 9601073 |
0.348 |
|
| 1998 |
Pollock WB, Rosell FI, Twitchett MB, Dumont ME, Mauk AG. Bacterial expression of a mitochondrial cytochrome c. Trimethylation of lys72 in yeast iso-1-cytochrome c and the alkaline conformational transition. Biochemistry. 37: 6124-31. PMID 9558351 DOI: 10.1021/Bi972188D |
0.371 |
|
| 1998 |
Döpner S, Hildebrandt P, Rosell aFI, Mauk AG. Alkaline Conformational Transitions of Ferricytochrome c Studied by Resonance Raman Spectroscopy Journal of the American Chemical Society. 120: 11246-11255. DOI: 10.1021/Ja9717572 |
0.347 |
|
| 1998 |
Rosell FI, Ferrer aJC, Mauk AG. Proton-Linked Protein Conformational Switching: Definition of the Alkaline Conformational Transition of Yeast Iso-1-ferricytochrome c‡ Journal of the American Chemical Society. 120: 11234-11245. DOI: 10.1021/Ja971756+ |
0.377 |
|
| 1997 |
Hunter CL, Lloyd E, Eltis LD, Rafferty SP, Lee H, Smith M, Mauk AG. Role of the heme propionates in the interaction of heme with apomyoglobin and apocytochrome b5. Biochemistry. 36: 1010-7. PMID 9033390 DOI: 10.1021/bi961385u |
0.524 |
|
| 1997 |
Bujons J, Dikiy A, Ferrer JC, Banci L, Mauk AG. Charge reversal of a critical active-site residue of cytochrome-c peroxidase: characterization of the Arg48-->Glu variant. European Journal of Biochemistry / Febs. 243: 72-84. PMID 9030724 DOI: 10.1111/J.1432-1033.1997.72_1A.X |
0.415 |
|
| 1997 |
Twitchett MB, Ferrer JC, Siddarth aP, Mauk AG. Intramolecular Electron Transfer Kinetics of a Synthetic Flavocytochrome c Journal of the American Chemical Society. 119: 435-436. DOI: 10.1021/Ja963086Y |
0.385 |
|
| 1996 |
Rafferty SP, Guillemette JG, Berghuis AM, Smith M, Brayer GD, Mauk AG. Mechanistic and structural contributions of critical surface and internal residues to cytochrome c electron transfer reactivity. Biochemistry. 35: 10784-92. PMID 8718869 DOI: 10.1021/bi960430v |
0.346 |
|
| 1996 |
Rafferty SP, Srnith M, Mauk AG. Azide binding and active site dynamics of position-82 variants of ferricytochrome c Inorganica Chimica Acta. 242: 171-177. DOI: 10.1016/0020-1693(95)04863-4 |
0.364 |
|
| 1995 |
Mauk AG, Mauk MR, Moore GR, Northrup SH. Experimental and theoretical analysis of the interaction between cytochrome c and cytochrome b5. Journal of Bioenergetics and Biomembranes. 27: 311-30. PMID 8847345 DOI: 10.1007/Bf02110101 |
0.319 |
|
| 1995 |
Hildebrand DP, Ferrer JC, Tang HL, Smith M, Mauk AG. Trans effects on cysteine ligation in the proximal His93Cys variant of horse heart myoglobin Biochemistry. 34: 11598-11605. PMID 7547891 DOI: 10.1016/0162-0134(95)97525-U |
0.371 |
|
| 1995 |
Lloyd E, Hildebrand DP, Tu KM, Mauk AG. Conversion of myoglobin into a reversible electron transfer protein that maintains bishistidine axial ligation Journal of the American Chemical Society. 117: 6434-6438. DOI: 10.1021/Ja00129A003 |
0.421 |
|
| 1995 |
Bujons J, Mauk MR, Mauk AG. Mutagenic evidence concerning the location of two binding sites for cytochrome C on the surface of cytochrome C peroxidase Journal of Inorganic Biochemistry. 59: 432. DOI: 10.1016/0162-0134(95)97528-X |
0.363 |
|
| 1995 |
Rosell FI, Mauk AG. pH-dependent conformational dynamics of alkaline ferricytochrome C Journal of Inorganic Biochemistry. 59: 430. DOI: 10.1016/0162-0134(95)97526-V |
0.324 |
|
| 1995 |
Nocek JM, Zhou JS, DeVan ML, Sishta BP, Casey JR, Mauk A, Hoffman BM. Cyclic electron transfer within the 1:1 [Zn-deutero-myoglobin, cytochrome B5] complex and the 2:1 [cytochrome C, cytochrome C peroxidase] complex Journal of Inorganic Biochemistry. 59: 267. DOI: 10.1016/0162-0134(95)97370-6 |
0.434 |
|
| 1995 |
Torres E, Sandoval JV, Rosell FI, Mauk AG, Vazquez-Duhalt R. Site-directed mutagenesis improves the biocatalytic activity of iso-1-cytochrome c in polycyclic hydrocarbon oxidation Enzyme and Microbial Technology. 17: 1014-1020. DOI: 10.1016/0141-0229(95)00032-1 |
0.413 |
|
| 1994 |
Kornblatt JA, Kornblatt MJ, Hoa GH, Mauk AG. Responses of two protein-protein complexes to solvent stress: does water play a role at the interface? Biophysical Journal. 65: 1059-65. PMID 8241386 DOI: 10.1016/S0006-3495(93)81168-8 |
0.318 |
|
| 1994 |
Tang HL, Chance B, Mauk AG, Powers LS, Reddy KS, Smith M. Spectroscopic, electrochemical, and ligand binding properties of the horse heart metmyoglobin His64-Tyr variant. Biochimica Et Biophysica Acta. 1206: 90-6. PMID 8186254 DOI: 10.1016/0167-4838(94)90076-0 |
0.352 |
|
| 1994 |
Lloyd E, Mauk AG. Formation of sulphmyoglobin during expression of horse heart myoglobin in Escherichia coli. Febs Letters. 340: 281-6. PMID 8131859 DOI: 10.1016/0014-5793(94)80154-1 |
0.332 |
|
| 1994 |
Ferrer JC, Turano P, Banci L, Bertini I, Morris IK, Smith KM, Smith M, Mauk AG. Active site coordination chemistry of the cytochrome c peroxidase Asp235Ala variant: spectroscopic and functional characterization. Biochemistry. 33: 7819-29. PMID 8011646 DOI: 10.1021/bi00191a009 |
0.317 |
|
| 1994 |
Lloyd E, Ferrer JC, Funk WD, Mauk MR, Mauk AG. Recombinant human erythrocyte cytochrome b5. Biochemistry. 33: 11432-7. PMID 7918357 |
0.303 |
|
| 1994 |
Guillemette JG, Barker PD, Eltis LD, Lo TP, Smith M, Brayer GD, Mauk AG. Analysis of the bimolecular reduction of ferricytochrome c by ferrocytochrome b5 through mutagenesis and molecular modelling. Biochimie. 76: 592-604. PMID 7893811 DOI: 10.1016/0300-9084(94)90136-8 |
0.601 |
|
| 1993 |
Hildebrandt P, Vanhecke F, Buse G, Soulimane T, Mauk AG. Resonance Raman study of the interactions between cytochrome c variants and cytochrome c oxidase. Biochemistry. 32: 10912-22. PMID 8399241 |
0.345 |
|
| 1993 |
Northrup SH, Thomasson KA, Miller CM, Barker PD, Eltis LD, Guillemette JG, Inglis SC, Mauk AG. Effects of charged amino acid mutations on the bimolecular kinetics of reduction of yeast iso-1-ferricytochrome c by bovine ferrocytochrome b5. Biochemistry. 32: 6613-23. PMID 8392365 |
0.53 |
|
| 1993 |
Davies AM, Guillemette JG, Smith M, Greenwood C, Thurgood AG, Mauk AG, Moore GR. Redesign of the interior hydrophilic region of mitochondrial cytochrome c by site-directed mutagenesis. Biochemistry. 32: 5431-5. PMID 8388720 DOI: 10.1021/Bi00071A019 |
0.312 |
|
| 1993 |
Meyer TE, Rivera M, Walker FA, Mauk MR, Mauk AG, Cusanovich MA, Tollin G. Laser flash photolysis studies of electron transfer to the cytochrome b5-cytochrome c complex. Biochemistry. 32: 622-7. PMID 8380703 DOI: 10.1021/BI00053A030 |
0.354 |
|
| 1993 |
Ferrer JC, Guillemette JG, Bogumil R, Inglis SC, Smith M, Mauk AG. Identification of Lys79 as an iron ligand in one form of alkaline yeast iso-1-ferricytochrome c Journal of the American Chemical Society. 115: 7507-7508. DOI: 10.1021/Ja00069A062 |
0.357 |
|
| 1992 |
Hazzard JT, Mauk AG, Tollin G. Laser flash photolysis studies of electron transfer mechanisms in cytochromes: an aromatic residue at position 82 is not required for cytochrome c reduction by flavin semiquinones or electron transfer from cytochrome c to cytochrome oxidase. Archives of Biochemistry and Biophysics. 298: 91-95. PMID 1326255 DOI: 10.1016/0003-9861(92)90098-H |
0.439 |
|
| 1992 |
Barker PD, Mauk AG. PH-linked conformational regulation of a metalloprotein oxidation-reduction equilibrium : electrochemical analysis of the alkaline form of cytochrome c Journal of the American Chemical Society. 114: 3619-3624. DOI: 10.1021/Ja00036A006 |
0.425 |
|
| 1991 |
Eltis LD, Herbert RG, Barker PD, Mauk AG, Northrup SH. Reduction of horse heart ferricytochrome c by bovine liver ferrocytochrome b5. Experimental and theoretical analysis. Biochemistry. 30: 3663-74. PMID 1849735 DOI: 10.1021/Bi00229A011 |
0.578 |
|
| 1991 |
Thurgood AG, Davies AM, Greenwood C, Mauk AG, Smith M, Guillemette JG, Moore GR. NMR study of the structural characteristics of variants of yeast iso-1-cytochrome c in which unvaried aromatic residues have been substituted. European Journal of Biochemistry / Febs. 202: 339-47. PMID 1662130 DOI: 10.1111/J.1432-1033.1991.Tb16381.X |
0.384 |
|
| 1991 |
DePillis GD, Sishta BP, Mauk AG, Ortiz de Montellano PR. Small substrates and cytochrome c are oxidized at different sites of cytochrome c peroxidase. The Journal of Biological Chemistry. 266: 19334-41. PMID 1655784 |
0.301 |
|
| 1991 |
Mauk MR, Barker PD, Mauk AG. Proton linkage of complex formation between cytochrome c and cytochrome b5: electrostatic consequences of protein-protein interactions. Biochemistry. 30: 9873-81. PMID 1655024 DOI: 10.1021/bi00105a010 |
0.32 |
|
| 1991 |
Thurgood AG, Pielak GJ, Cutler RL, Davies AM, Greenwood C, Mauk AG, Smith M, Williamson DJ, Moore GR. Change in charge of an unvaried heme contact residue does not cause a major change of conformation in cytochrome c. Febs Letters. 284: 173-7. PMID 1647980 DOI: 10.1016/0014-5793(91)80678-V |
0.361 |
|
| 1991 |
Ferrer JC, Ring M, Mauk AG. Recombinant cytochrome c peroxidase folds properly without conformational "annealing". Biochemical and Biophysical Research Communications. 176: 1469-1472. PMID 1645545 DOI: 10.1016/0006-291X(91)90452-D |
0.405 |
|
| 1991 |
Goodin DB, Davidson MG, Roe JA, Mauk AG, Smith M. Amino acid substitutions at tryptophan-51 of cytochrome c peroxidase: effects on coordination, species preference for cytochrome c, and electron transfer. Biochemistry. 30: 4953-62. PMID 1645185 DOI: 10.1021/BI00234A017 |
0.302 |
|
| 1991 |
Jacobs BA, Mauk MR, Funk WD, MacGillivray RTA, Mauk AG, Gray HB. Preparation, characterization, and intramolecular electron transfer in pentaammineruthenium histidine-26 cytochrome b5 derivatives: role of the intervening medium in long-range donor-acceptor electronic coupling Journal of the American Chemical Society. 113: 4390-4394. DOI: 10.1021/Ja00012A003 |
0.467 |
|
| 1991 |
Banci L, Bertini I, Turano P, Ferrer JC, Mauk AG. Comparative proton NMR study of ferric low-spin cytochrome c peroxidase and horseradish peroxidase Inorganic Chemistry. 30: 4510-4516. DOI: 10.1021/Ic00024A010 |
0.313 |
|
| 1991 |
Rafferty SP, Ferrer JC, Guillemette J, Smith M, Mauk A. Azide binding to position 82 mutants of yeast iso-1-ferricytochrome c Journal of Inorganic Biochemistry. 43: 316. DOI: 10.1016/0162-0134(91)84303-Q |
0.344 |
|
| 1991 |
Barker PD, Mauk MR, Mauk AG. Proton linkage of complex formation between cytochrome c and cytochrome b5 Journal of Inorganic Biochemistry. 43: 315. DOI: 10.1016/0162-0134(91)84302-P |
0.423 |
|
| 1991 |
Barker PD, Mylrajan M, Funk WD, MacGillivray RTA, Loehr TM, Mauk AG. Protoheme IX conversion to a chlorin by mutation of cytochrome b5 residue Asn-57 to cys. Journal of Inorganic Biochemistry. 43: 308. DOI: 10.1016/0162-0134(91)84295-K |
0.308 |
|
| 1991 |
Barker PD, Mauk MR, Mauk AG. Electrostatic properties of cytochrome c variants and of the cytochrome c-cytochrome b5 complex. Journal of Inorganic Biochemistry. 43: 294. DOI: 10.1016/0162-0134(91)84281-D |
0.418 |
|
| 1990 |
Burch AM, Rigby SE, Funk WD, MacGillivray RT, Mauk MR, Mauk AG, Moore GR. NMR characterization of surface interactions in the cytochrome b5-cytochrome c complex. Science (New York, N.Y.). 247: 831-3. PMID 2154849 DOI: 10.1126/SCIENCE.2154849 |
0.341 |
|
| 1990 |
Funk WD, Lo TP, Mauk MR, Brayer GD, MacGillivray RT, Mauk AG. Mutagenic, electrochemical, and crystallographic investigation of the cytochrome b5 oxidation-reduction equilibrium: involvement of asparagine-57, serine-64, and heme propionate-7. Biochemistry. 29: 5500-8. PMID 2117468 DOI: 10.1021/Bi00475A013 |
0.312 |
|
| 1990 |
Nocek JM, Liang N, Wallin SA, Mauk AG, Hoffman BM. Low-temperature conformational transition within the [zinc-cytochrome c peroxidase, cytochrome c] electron-transfer complex Journal of the American Chemical Society. 112: 1623-1625. DOI: 10.1021/Ja00160A049 |
0.407 |
|
| 1989 |
Mauk MR, Mauk AG. Crosslinking of cytochrome c and cytochrome b5 with a water-soluble carbodiimide. Reaction conditions, product analysis and critique of the technique. Febs Journal. 186: 473-483. PMID 2558010 DOI: 10.1111/J.1432-1033.1989.Tb15231.X |
0.418 |
|
| 1989 |
Cutler RL, Davies AM, Creighton S, Warshel A, Moore GR, Smith M, Mauk AG. Role of arginine-38 in regulation of the cytochrome c oxidation-reduction equilibrium. Biochemistry. 28: 3188-97. PMID 2545252 DOI: 10.1021/Bi00434A012 |
0.434 |
|
| 1989 |
Pearce LL, Gartner AL, Smith M, Mauk AG. Mutation-induced perturbation of the cytochrome c alkaline transition. Biochemistry. 28: 3152-3156. PMID 2545249 DOI: 10.1021/Bi00434A006 |
0.417 |
|
| 1989 |
Michel B, Mauk AG, Bosshard HR. Binding and oxidation of mutant cytochromes c by cytochrome-c oxidase. Febs Letters. 243: 149-52. PMID 2537228 DOI: 10.1016/0014-5793(89)80118-8 |
0.31 |
|
| 1989 |
Mauk A, Nocek J, Stemp E, Margoliash E, Hoffman B. Regulation of interprotein electron transfer within the Zn- cytochrome c peroxidase/cytochrome c complex by a conformational gate Journal of Inorganic Biochemistry. 36: 213. DOI: 10.1016/0162-0134(89)84196-0 |
0.311 |
|
| 1989 |
Mauk A, Stemp E, Nocek J, Margoliash E, Hoffman B. Structural basis for conformational gating of electron transfer in zinc-cytochrome c peroxidase/cytochrome c complexes Journal of Inorganic Biochemistry. 36: 212. DOI: 10.1016/0162-0134(89)84193-5 |
0.321 |
|
| 1989 |
Eltis L, Barker P, Mauk A. Ferrocytochrome b5 reduction of ferricytochrome c Journal of Inorganic Biochemistry. 36: 211. DOI: 10.1016/0162-0134(89)84191-1 |
0.553 |
|
| 1989 |
Jacobs BA, Clair CSS, Mauk MR, Mauk AG, Gray HB. Electron transfer in heme and blue-copper proteins: ruthenium-modified cytochrome b5 and azurin Journal of Inorganic Biochemistry. 36: 210. DOI: 10.1016/0162-0134(89)84188-1 |
0.438 |
|
| 1988 |
Eltis L, Mauk AG, Hazzard JT, Cusanovich MA, Tollin G. Kinetics of flavin semiquinone reduction of the components of the cytochrome c-cytochrome b5 complex. Biochemistry. 27: 5455-60. PMID 2846038 DOI: 10.1021/bi00415a011 |
0.6 |
|
| 1988 |
Liang N, Mauk AG, Pielak GJ, Johnson JA, Smith M, Hoffman BM. Regulation of interprotein electron transfer by residue 82 of yeast cytochrome c. Science (New York, N.Y.). 240: 311-3. PMID 2832950 DOI: 10.1126/Science.2832950 |
0.318 |
|
| 1988 |
Burch AM, Rigby SEJ, Funk W, Macgillivray RTA, Mauk AG, Mauk M, Moore GR. A 13C nuclear-magnetic-resonance investigation of the interaction between cytochrome c and cytochrome b5 Biochemical Society Transactions. 16: 844-845. DOI: 10.1042/Bst0160844A |
0.368 |
|
| 1988 |
DAVIES AM, CUTLER RL, SMITH M, MAUK AG, THURGOOD AGP, MOORE GR. Structure of yeast iso-1-cytochrome c in which arginine-38 is replaced by alanine-38 Biochemical Society Transactions. 16: 844-844. DOI: 10.1042/Bst0160844 |
0.367 |
|
| 1988 |
Kornblatt JA, Hui Bon Hoa G, Eltis L, Mauk AG. The effects of pressure on porphyrin c-cytochrome b5 complex formation Journal of the American Chemical Society. 110: 5909-5911. DOI: 10.1021/Ja00225A058 |
0.581 |
|
| 1987 |
Hartshorn RT, Mauk AG, Mauk MR, Moore GR. NMR study of the interaction between cytochrome b5 and cytochrome c. Observation of a ternary complex formed by the two proteins and [Cr(en)3]3+. Febs Letters. 213: 391-5. PMID 3030818 DOI: 10.1016/0014-5793(87)81528-4 |
0.399 |
|
| 1987 |
Liang N, Pielak GJ, Mauk AG, Smith M, Hoffman BM. Yeast cytochrome c with phenylalanine or tyrosine at position 87 transfers electrons to (zinc cytochrome c peroxidase)+ at a rate ten thousand times that of the serine-87 or glycine-87 variants. Proceedings of the National Academy of Sciences of the United States of America. 84: 1249-52. PMID 3029774 DOI: 10.1073/Pnas.84.5.1249 |
0.328 |
|
| 1986 |
Mauk MR, Mauk AG, Weber PC, Matthew JB. Electrostatic analysis of the interaction of cytochrome c with native and dimethyl ester heme substituted cytochrome b5 Biochemistry. 25: 7085-7091. PMID 3026446 DOI: 10.1021/BI00370A049 |
0.351 |
|
| 1985 |
Pasternack RF, Gibbs EJ, Mauk AG, Reid LS, Wong NM, Kurokawa K, Hashim M, Muller-Eberhard U. Kinetics of hemoprotein reduction and interprotein heme transfer. Biochemistry. 24: 5443-8. PMID 4074707 DOI: 10.1021/Bi00341A024 |
0.35 |
|
| 1985 |
Pielak GJ, Mauk AG, Smith M. Site-directed mutagenesis of cytochrome c shows that an invariant Phe is not essential for function. Nature. 313: 152-4. PMID 2981414 DOI: 10.1038/313152A0 |
0.439 |
|
| 1985 |
McLendon GL, Winkler JR, Nocera DG, Mauk MR, Mauk AG, Gray HB. Quenching of zinc-substituted cytochrome c excited states by cytochrome b5 Journal of the American Chemical Society. 107: 739-740. DOI: 10.1021/Ja00289A055 |
0.665 |
|
| 1985 |
Scott RA, Mauk AG, Gray HB. Experimental approaches to studying biological electron transfer Journal of Chemical Education. 62: 932. DOI: 10.1021/Ed062P932 |
0.437 |
|
| 1984 |
Simolo KP, McLendon GL, Mauk MR, Mauk AG. Photoinduced electron transfer within a protein-protein complex formed between physiological redox partners: reduction of ferricytochrome b5 by the hemoglobin derivative .alpha.2Zn.beta.2Fe(III)CN Journal of the American Chemical Society. 106: 5012-5013. DOI: 10.1021/Ja00329A067 |
0.357 |
|
| 1982 |
Mauk AG, Bordignon E, Gray HB. Analysis of the kinetics of electron transfer between blue copper proteins and inorganic redox agents. Reactions involving bis(dipicolinate) complexes of cobalt(III) and iron(II) and stellacyanin, plastocyanin, and azurin Journal of the American Chemical Society. 104: 7654-7657. DOI: 10.1021/Ja00390A045 |
0.48 |
|
| 1982 |
Reid LS, Taniguchi VT, Gray HB, Mauk AG. Oxidation-reduction equilibrium of cytochrome b5 Journal of the American Chemical Society. 104: 7516-7519. DOI: 10.1021/Ja00390A021 |
0.454 |
|
| 1982 |
Reid LS, Mauk AG. Kinetics analysis of cytochrome b5 reduction by (ethylenediaminetetraacetato)ferrate(2-) ion Journal of the American Chemical Society. 104: 841-845. DOI: 10.1021/Ja00367A032 |
0.311 |
|
| 1980 |
Loehr JS, Loehr TM, Mauk AG, Gray HB. An electronic spectroscopic study of iron coordination in hemerythrin Journal of the American Chemical Society. 102: 6992-6996. DOI: 10.1021/Ja00543A015 |
0.435 |
|
| 1980 |
Mauk AG, Scott RA, Gray HB. Distances of electron transfer to and from metalloprotein redox sites in reactions with inorganic complexes Journal of the American Chemical Society. 102: 4360-4363. DOI: 10.1021/Ja00533A012 |
0.454 |
|
| 1980 |
Holwerda RA, Knaff DB, Gray HB, Clemmer JD, Crowley R, Smith JM, Mauk AG. Comparison of the electron-transfer reactivities of tris(oxalato)cobaltate(III) (Co(ox)33-) and tris(1,10-phenanthroline)cobalt(III) (Co(phen)33+) with metalloproteins Journal of the American Chemical Society. 102: 1142-1146. DOI: 10.1021/Ja00523A034 |
0.446 |
|
| 1979 |
Mauk AG, Gray HB. Analysis of the kinetics of electron transfer reactions of hemoglobin and myoglobin with inorganic complexes. Biochemical and Biophysical Research Communications. 86: 206-10. PMID 107952 DOI: 10.1016/0006-291X(79)90401-7 |
0.345 |
|
| 1979 |
Mauk AG, Coyle CL, Bordignon E, Gray HB. Bis(dipicolinate) complexes of cobalt(III) and iron(II) as new probes of metalloprotein electron-transfer reactivity. Analysis of reactions involving cytochrome c and cytochrome c551 Journal of the American Chemical Society. 101: 5054-5056. DOI: 10.1021/Ja00511A041 |
0.528 |
|
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