| Year |
Citation |
Score |
| 2011 |
Cheng Z, Zhang J, Ballou DP, Williams CH. Reactivity of thioredoxin as a protein thiol-disulfide oxidoreductase. Chemical Reviews. 111: 5768-83. PMID 21793530 DOI: 10.1021/Cr100006X |
0.453 |
|
| 2011 |
Huang HH, Day L, Cass CL, Ballou DP, Williams CH, Williams DL. Investigations of the catalytic mechanism of thioredoxin glutathione reductase from Schistosoma mansoni. Biochemistry. 50: 5870-82. PMID 21630672 DOI: 10.1021/Bi200107N |
0.441 |
|
| 2008 |
Huang HH, Arscott LD, Ballou DP, Williams CH. Function of Glu-469' in the acid-base catalysis of thioredoxin reductase from Drosophila melanogaster. Biochemistry. 47: 12769-76. PMID 18991392 DOI: 10.1021/Bi801449H |
0.514 |
|
| 2008 |
Huang HH, Arscott LD, Ballou DP, Williams CH. Acid-base catalysis in the mechanism of thioredoxin reductase from Drosophila melanogaster. Biochemistry. 47: 1721-31. PMID 18211101 DOI: 10.1021/Bi702040U |
0.485 |
|
| 2007 |
Cheng Z, Arscott LD, Ballou DP, Williams CH. The relationship of the redox potentials of thioredoxin and thioredoxin reductase from Drosophila melanogaster to the enzymatic mechanism: reduced thioredoxin is the reductant of glutathione in Drosophila. Biochemistry. 46: 7875-85. PMID 17550271 DOI: 10.1021/Bi700442R |
0.414 |
|
| 2006 |
McMillan PJ, Arscott LD, Ballou DP, Becker K, Williams CH, Müller S. Identification of acid-base catalytic residues of high-Mr thioredoxin reductase from Plasmodium falciparum. The Journal of Biological Chemistry. 281: 32967-77. PMID 16950793 DOI: 10.1074/Jbc.M601141200 |
0.491 |
|
| 2006 |
Johansson L, Arscott LD, Ballou DP, Williams CH, Arnér ES. Studies of an active site mutant of the selenoprotein thioredoxin reductase: the Ser-Cys-Cys-Ser motif of the insect orthologue is not sufficient to replace the Cys-Sec dyad in the mammalian enzyme. Free Radical Biology & Medicine. 41: 649-56. PMID 16863998 DOI: 10.1016/J.Freeradbiomed.2006.05.005 |
0.483 |
|
| 2005 |
Deponte M, Urig S, Arscott LD, Fritz-Wolf K, Réau R, Herold-Mende C, Koncarevic S, Meyer M, Davioud-Charvet E, Ballou DP, Williams CH, Becker K. Mechanistic studies on a novel, highly potent gold-phosphole inhibitor of human glutathione reductase. The Journal of Biological Chemistry. 280: 20628-37. PMID 15792952 DOI: 10.1074/Jbc.M412519200 |
0.4 |
|
| 2004 |
Eisenreich W, Kemter K, Bacher A, Mulrooney SB, Williams CH, Müller F. 13C-, 15N- and 31P-NMR studies of oxidized and reduced low molecular mass thioredoxin reductase and some mutant proteins. European Journal of Biochemistry / Febs. 271: 1437-52. PMID 15066170 DOI: 10.1111/J.1432-1033.2004.04043.X |
0.372 |
|
| 2003 |
Davioud-Charvet E, McLeish MJ, Veine DM, Giegel D, Arscott LD, Andricopulo AD, Becker K, Müller S, Schirmer RH, Williams CH, Kenyon GL. Mechanism-based inactivation of thioredoxin reductase from Plasmodium falciparum by Mannich bases. Implication for cytotoxicity. Biochemistry. 42: 13319-30. PMID 14609342 DOI: 10.1021/Bi0353629 |
0.434 |
|
| 2003 |
Gromer S, Johansson L, Bauer H, Arscott LD, Rauch S, Ballou DP, Williams CH, Schirmer RH, Arnér ES. Active sites of thioredoxin reductases: why selenoproteins? Proceedings of the National Academy of Sciences of the United States of America. 100: 12618-23. PMID 14569031 DOI: 10.1073/Pnas.2134510100 |
0.496 |
|
| 2003 |
Bauer H, Massey V, Arscott LD, Schirmer RH, Ballou DP, Williams CH. The mechanism of high Mr thioredoxin reductase from Drosophila melanogaster. The Journal of Biological Chemistry. 278: 33020-8. PMID 12816954 DOI: 10.1074/Jbc.M303762200 |
0.71 |
|
| 2003 |
Williams CH, Ballou DP. Vincent Massey 28 November 1926 – 26 August 2002 Elected FRS 1977 Biographical Memoirs of Fellows of the Royal Society. 49: 335-350. DOI: 10.1098/Rsbm.2003.0019 |
0.356 |
|
| 2000 |
Williams CH, Arscott LD, Müller S, Lennon BW, Ludwig ML, Wang PF, Veine DM, Becker K, Schirmer RH. Thioredoxin reductase two modes of catalysis have evolved. European Journal of Biochemistry / Febs. 267: 6110-7. PMID 11012662 DOI: 10.1046/j.1432-1327.2000.01702.x |
0.341 |
|
| 2000 |
Williams CH. Thioredoxin-thioredoxin reductase--a system that has come of age. European Journal of Biochemistry / Febs. 267: 6101. PMID 11012660 DOI: 10.1046/J.1432-1327.2000.01700.X |
0.456 |
|
| 2000 |
Bohme CC, Arscott LD, Becker K, Schirmer RH, Williams CH. Kinetic characterization of glutathione reductase from the malarial parasite Plasmodium falciparum. Comparison with the human enzyme. The Journal of Biological Chemistry. 275: 37317-23. PMID 10969088 DOI: 10.1074/Jbc.M007695200 |
0.461 |
|
| 2000 |
Lennon BW, Williams CH, Ludwig ML. Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase. Science (New York, N.Y.). 289: 1190-4. PMID 10947986 DOI: 10.1126/Science.289.5482.1190 |
0.412 |
|
| 2000 |
Arscott LD, Veine DM, Williams CH. Mixed disulfide with glutathione as an intermediate in the reaction catalyzed by glutathione reductase from yeast and as a major form of the enzyme in the cell. Biochemistry. 39: 4711-21. PMID 10769127 DOI: 10.1021/Bi9926431 |
0.49 |
|
| 1999 |
Lennon BW, Williams CH, Ludwig ML. Crystal structure of reduced thioredoxin reductase from Escherichia coli: structural flexibility in the isoalloxazine ring of the flavin adenine dinucleotide cofactor. Protein Science : a Publication of the Protein Society. 8: 2366-79. PMID 10595539 DOI: 10.1110/Ps.8.11.2366 |
0.395 |
|
| 1999 |
Sanders SA, Williams CH, Massey V. The roles of two amino acid residues in the active site of L-lactate monooxygenase. Mutation of arginine 187 to methionine and histidine 240 to glutamine. The Journal of Biological Chemistry. 274: 22289-95. PMID 10428797 DOI: 10.1074/Jbc.274.32.22289 |
0.718 |
|
| 1999 |
Wang PF, Arscott LD, Gilberger TW, Müller S, Williams CH. Thioredoxin reductase from Plasmodium falciparum: evidence for interaction between the C-terminal cysteine residues and the active site disulfide-dithiol. Biochemistry. 38: 3187-96. PMID 10074374 DOI: 10.1021/bi982674g |
0.394 |
|
| 1998 |
Wang PF, Marcinkeviciene J, Williams CH, Blanchard JS. Thioredoxin reductase-thioredoxin fusion enzyme from Mycobacterium leprae: comparison with the separately expressed thioredoxin reductase. Biochemistry. 37: 16378-89. PMID 9819230 DOI: 10.1021/Bi980754E |
0.447 |
|
| 1998 |
Veine DM, Arscott LD, Williams CH. Redox potentials for yeast, Escherichia coli and human glutathione reductase relative to the NAD+/NADH redox couple: enzyme forms active in catalysis. Biochemistry. 37: 15575-82. PMID 9799522 DOI: 10.1021/bi9811314 |
0.307 |
|
| 1998 |
Krauth-Siegel RL, Arscott LD, Schönleben-Janas A, Schirmer RH, Williams CH. Role of active site tyrosine residues in catalysis by human glutathione reductase. Biochemistry. 37: 13968-77. PMID 9760231 DOI: 10.1021/bi980637j |
0.38 |
|
| 1998 |
Gromer S, Arscott LD, Williams CH, Schirmer RH, Becker K. Human placenta thioredoxin reductase. Isolation of the selenoenzyme, steady state kinetics, and inhibition by therapeutic gold compounds. The Journal of Biological Chemistry. 273: 20096-101. PMID 9685351 DOI: 10.1074/Jbc.273.32.20096 |
0.392 |
|
| 1998 |
Veine DM, Mulrooney SB, Wang PF, Williams CH. Formation and properties of mixed disulfides between thioredoxin reductase from Escherichia coli and thioredoxin: evidence that cysteine-138 functions to initiate dithiol-disulfide interchange and to accept the reducing equivalent from reduced flavin. Protein Science : a Publication of the Protein Society. 7: 1441-50. PMID 9655349 DOI: 10.1002/Pro.5560070621 |
0.416 |
|
| 1998 |
Veine DM, Ohnishi K, Williams CH. Thioredoxin reductase from Escherichia coli: evidence of restriction to a single conformation upon formation of a crosslink between engineered cysteines. Protein Science : a Publication of the Protein Society. 7: 369-75. PMID 9521113 DOI: 10.1002/Pro.5560070217 |
0.454 |
|
| 1998 |
Färber PM, Arscott LD, Williams CH, Becker K, Schirmer RH. Recombinant Plasmodium falciparum glutathione reductase is inhibited by the antimalarial dye methylene blue. Febs Letters. 422: 311-4. PMID 9498806 DOI: 10.1016/S0014-5793(98)00031-3 |
0.395 |
|
| 1997 |
Sun W, Williams CH, Massey V. The role of glycine 99 in L-lactate monooxygenase from Mycobacterium smegmatis. The Journal of Biological Chemistry. 272: 27065-76. PMID 9341146 DOI: 10.1074/Jbc.272.43.27065 |
0.696 |
|
| 1997 |
Mulrooney SB, Williams CH. Evidence for two conformational states of thioredoxin reductase from Escherichia coli: use of intrinsic and extrinsic quenchers of flavin fluorescence as probes to observe domain rotation. Protein Science : a Publication of the Protein Society. 6: 2188-95. PMID 9336841 DOI: 10.1002/Pro.5560061013 |
0.365 |
|
| 1997 |
Lennon BW, Williams CH. Reductive half-reaction of thioredoxin reductase from Escherichia coli. Biochemistry. 36: 9464-77. PMID 9235991 DOI: 10.1021/Bi970307J |
0.444 |
|
| 1997 |
Arscott LD, Gromer S, Schirmer RH, Becker K, Williams CH. The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America. 94: 3621-6. PMID 9108027 DOI: 10.1073/Pnas.94.8.3621 |
0.44 |
|
| 1996 |
Bashir A, Arscott LD, Perham RN, Williams CH, Berry A. The oxidative and reductive half reactions of subunit interface mutants of Escherichia coli glutathione reductase. Biochemical Society Transactions. 24: 9S. PMID 8674773 DOI: 10.1042/Bst024009S |
0.51 |
|
| 1996 |
Wang PF, Veine DM, Ahn SH, Williams CH. A stable mixed disulfide between thioredoxin reductase and its substrate, thioredoxin: preparation and characterization. Biochemistry. 35: 4812-9. PMID 8664271 DOI: 10.1021/Bi9526793 |
0.402 |
|
| 1996 |
Lennon BW, Williams CH. Enzyme-monitored turnover of Escherichia coli thioredoxin reductase: insights for catalysis. Biochemistry. 35: 4704-12. PMID 8664260 DOI: 10.1021/Bi952521I |
0.479 |
|
| 1996 |
Sun W, Williams CH, Massey V. Site-directed mutagenesis of glycine 99 to alanine in L-lactate monooxygenase from Mycobacterium smegmatis. The Journal of Biological Chemistry. 271: 17226-33. PMID 8663383 DOI: 10.1074/Jbc.271.29.17226 |
0.681 |
|
| 1995 |
Lennon BW, Williams CH. Effect of pyridine nucleotide on the oxidative half-reaction of Escherichia coli thioredoxin reductase Biochemistry. 34: 3670-3677. PMID 7893663 DOI: 10.1021/Bi00011A023 |
0.416 |
|
| 1995 |
Williams CH. Mechanism and structure of thioredoxin reductase from Escherichia coli Faseb Journal. 9: 1267-1276. PMID 7557016 DOI: 10.1096/Fasebj.9.13.7557016 |
0.411 |
|
| 1995 |
Williams CH. Lipoamide dehydrogenase from escherichia coli lacking the redox active bisulfide: C44S and C49S. Redox properties of the FAD and interactions with pyridine nucleotides Biochemistry. 34: 11766-11776. PMID 7547909 DOI: 10.1021/Bi00037A014 |
0.419 |
|
| 1995 |
Williams CH. Characterization of lipoamide dehydrogenase from escherichia coli lacking the redox active disulfide: C44S and C49S 1 Biochemistry. 34: 11757-11765. PMID 7547908 DOI: 10.1021/Bi00037A013 |
0.437 |
|
| 1994 |
Maeda-Yorita K, Russell GC, Guest JR, Massey V, Williams CH. Modulation of the oxidation-reduction potential of the flavin in lipoamide dehydrogenase from Escherichia coli by alteration of a nearby charged residue, K53R. Biochemistry. 33: 6213-20. PMID 8193135 DOI: 10.1021/Bi00186A022 |
0.701 |
|
| 1994 |
Mulrooney SB, Williams CH. Potential active-site base of thioredoxin reductase from Escherichia coli: Examination of histidine245 and aspartate139 by site-directed mutagenesis Biochemistry. 33: 3148-3154. PMID 8136348 DOI: 10.1021/Bi00177A002 |
0.433 |
|
| 1994 |
Müh U, Williams CH, Massey V. Lactate monooxygenase. III. Additive contributions of active site residues to catalytic efficiency and stabilization of an anionic transition state. The Journal of Biological Chemistry. 269: 7994-8000. PMID 8132520 |
0.701 |
|
| 1994 |
Müh U, Williams CH, Massey V. Lactate monooxygenase. II. Site-directed mutagenesis of the postulated active site base histidine 290. The Journal of Biological Chemistry. 269: 7989-93. PMID 8132519 |
0.704 |
|
| 1994 |
Müh U, Massey V, Williams CH. Lactate monooxygenase. I. Expression of the mycobacterial gene in Escherichia coli and site-directed mutagenesis of lysine 266. The Journal of Biological Chemistry. 269: 7982-8. PMID 8132518 |
0.714 |
|
| 1994 |
Cenas NK, Arscott D, Williams CH, Blanchard JS. Mechanism of reduction of quinones by Trypanosoma congolense trypanothione reductase. Biochemistry. 33: 2509-15. PMID 8117712 DOI: 10.1021/Bi00175A021 |
0.445 |
|
| 1994 |
Waksman G, Krishna TSR, Williams CH, Kuriyan J. Crystal structure of Escherichia coli thioredoxin reductase refined at 2 Å resolution: Implications for a large conformational change during catalysis Journal of Molecular Biology. 236: 800-816. PMID 8114095 DOI: 10.2210/Pdb1Tde/Pdb |
0.45 |
|
| 1994 |
Rietveld P, Arscott LD, Berry A, Scrutton NS, Deonarain MP, Perham RN, Williams CH. Reductive and oxidative half-reactions of glutathione reductase from Escherichia coli. Biochemistry. 33: 13888-95. PMID 7947797 DOI: 10.1021/Bi00250A043 |
0.322 |
|
| 1992 |
Ennis MP, Irvine GB, Williams CH. Aminopeptidase activities present in tissues of Helix aspersa. Comparative Biochemistry and Physiology. B, Comparative Biochemistry. 99: 321-6. PMID 1764911 DOI: 10.1016/0305-0491(91)90049-J |
0.312 |
|
| 1992 |
Benen J, van Berkel W, Dieteren N, Arscott D, Williams C, Veeger C, de Kok A. Lipoamide dehydrogenase from Azotobacter vinelandii: site-directed mutagenesis of the His450-Glu455 diad. Kinetics of wild-type and mutated enzymes. European Journal of Biochemistry / Febs. 207: 487-97. PMID 1633804 DOI: 10.1111/J.1432-1033.1992.Tb17075.X |
0.512 |
|
| 1992 |
Prongay AJ, Williams CH. Oxidation-reduction properties of Escherichia coli thioredoxin reductase altered at each active site cysteine residue Journal of Biological Chemistry. 267: 25181-25188. PMID 1460018 |
0.414 |
|
| 1992 |
Macheroux P, Mulrooney SB, Williams CH, Massey V. Direct expression of active spinach glycolate oxidase in Escherichia coli. Biochimica Et Biophysica Acta. 1132: 11-6. PMID 1324737 DOI: 10.1016/0167-4781(92)90046-3 |
0.667 |
|
| 1991 |
Kuriyan J, Krishna TSR, Wong L, Guenther B, Pahler A, Williams CH, Model P. Convergent evolution of similar function in two structurally divergent enzymes Nature. 352: 172-174. PMID 2067578 DOI: 10.1038/352172A0 |
0.444 |
|
| 1991 |
Miller SM, Massey V, Williams CH, Ballou DP, Walsh CT. Communication between the active sites in dimeric mercuric ion reductase: an alternating sites hypothesis for catalysis. Biochemistry. 30: 2600-12. PMID 2001350 DOI: 10.1021/Bi00224A006 |
0.706 |
|
| 1991 |
Maeda-Yorita K, Russell GC, Guest JR, Massey V, Williams CH. Properties of lipoamide dehydrogenase altered by site-directed mutagenesis at a key residue (I184Y) in the pyridine nucleotide binding domain. Biochemistry. 30: 11788-95. PMID 1751496 DOI: 10.1021/Bi00115A008 |
0.721 |
|
| 1990 |
Giegel DA, Williams CH, Massey V. L-lactate 2-monooxygenase from Mycobacterium smegmatis. Cloning, nucleotide sequence, and primary structure homology within an enzyme family. The Journal of Biological Chemistry. 265: 6626-32. PMID 2324094 |
0.646 |
|
| 1990 |
Prongay AJ, Williams CH. Evidence for direct interaction between cysteine 138 and the flavin in thioredoxin reductase. A study using flavin analogs Journal of Biological Chemistry. 265: 18968-18975. PMID 2229055 |
0.327 |
|
| 1990 |
Miller SM, Massey V, Ballou D, Williams CH, Distefano MD, Moore MJ, Walsh CT. Use of a site-directed triple mutant to trap intermediates: demonstration that the flavin C(4a)-thiol adduct and reduced flavin are kinetically competent intermediates in mercuric ion reductase. Biochemistry. 29: 2831-41. PMID 2189497 DOI: 10.1021/Bi00463A028 |
0.724 |
|
| 1989 |
Williams CH, Lawson J, Backwell FR. Oxidation of 3-amino-1-phenylprop-1-enes by monoamine oxidase and their use in a continuous assay of the enzyme. The Biochemical Journal. 256: 911-5. PMID 3223960 DOI: 10.1042/bj2560911 |
0.311 |
|
| 1989 |
Arscott LD, Drake DM, Williams CH. Inactivation-reactivation of two-electron reduced Escherichia coli glutathione reductase involving a dimer-monomer equilibrium Biochemistry. 28: 3591-3598. PMID 2663073 |
0.357 |
|
| 1989 |
Sahlman L, Williams CH. Titration studies on the active sites of pig heart lipoamide dehydrogenase and yeast glutathione reductase as monitored by the charge transfer absorbance Journal of Biological Chemistry. 264: 8033-8038. PMID 2656672 |
0.325 |
|
| 1989 |
Miller SM, Moore MJ, Massey V, Williams CH, Distefano MD, Ballou DP, Walsh CT. Evidence for the participation of Cys558 and Cys559 at the active site of mercuric reductase. Biochemistry. 28: 1194-205. PMID 2653437 DOI: 10.1021/Bi00429A037 |
0.717 |
|
| 1989 |
Prongay AJ, Engelke DR, Williams CH. Characterization of two active site mutations of thioredoxin reductase from Escherichia coli Journal of Biological Chemistry. 264: 2656-2664. PMID 2644268 |
0.361 |
|
| 1989 |
Sahlman L, Williams CH. Lipoamide dehydrogenase from Escherichia coli. Steady-state kinetics of the physiological reaction Journal of Biological Chemistry. 264: 8039-8045. PMID 2498307 |
0.378 |
|
| 1988 |
Negri A, Massey V, Williams CH, Schopfer LM. The kinetic mechanism of beef kidney D-aspartate oxidase. The Journal of Biological Chemistry. 263: 13557-63. PMID 2901415 |
0.688 |
|
| 1987 |
Beattie RE, Elmore DT, Williams CH, Guthrie DJ. The behaviour of leucine aminopeptidase towards thionopeptides. The Biochemical Journal. 245: 285-8. PMID 3663153 DOI: 10.1042/bj2450285 |
0.312 |
|
| 1987 |
Negri A, Massey V, Williams CH. D-aspartate oxidase from beef kidney. Purification and properties. The Journal of Biological Chemistry. 262: 10026-34. PMID 3611051 |
0.692 |
|
| 1987 |
Giegel DA, Massey V, Williams CH. L-lactate-2-monooxygenase. Sequence of peptides containing residues modified by 1-fluoro-2,4-dinitrobenzene. The Journal of Biological Chemistry. 262: 5705-10. PMID 3571231 |
0.683 |
|
| 1987 |
D'Silva C, Williams CH, Massey V. Identification of methionine-110 as the residue covalently modified in the electrophilic inactivation of D-amino-acid oxidase by O-(2,4-dinitrophenyl) hydroxylamine. Biochemistry. 26: 1717-22. PMID 2885027 DOI: 10.1021/Bi00380A034 |
0.697 |
|
| 1986 |
Miller SM, Ballou DP, Massey V, Williams CH, Walsh CT. Two-electron reduced mercuric reductase binds Hg(II) to the active site dithiol but does not catalyze Hg(II) reduction. The Journal of Biological Chemistry. 261: 8081-4. PMID 3522563 |
0.697 |
|
| 1986 |
D'Silva C, Williams CH, Massey V. Electrophilic amination of a single methionine residue located at the active site of D-amino acid oxidase by O-(2,4-dinitrophenyl)hydroxylamine. Biochemistry. 25: 5602-8. PMID 2877687 DOI: 10.1021/Bi00367A039 |
0.742 |
|
| 1985 |
O'Donnell ME, Williams CH. Reaction of both active site thiols of reduced thioredoxin reductase with N-ethylmaleimide. Biochemistry. 24: 7617-21. PMID 3912005 DOI: 10.1021/Bi00347A018 |
0.589 |
|
| 1984 |
O'Donnell ME, Williams CH. Graphical analysis of interactions between oxidation-reduction sites in two site oxidation-reduction proteins. Analytical Biochemistry. 136: 235-46. PMID 6370035 DOI: 10.1016/0003-2697(84)90330-0 |
0.548 |
|
| 1984 |
O'Donnell ME, Williams CH. Reconstitution of Escherichia coli thioredoxin reductase with 1-deazaFAD. Evidence for 1-deazaFAD C-4a adduct formation linked to the ionization of an active site base. The Journal of Biological Chemistry. 259: 2243-51. PMID 6365906 |
0.48 |
|
| 1984 |
Swenson RP, Williams CH, Massey V. Methylation of the active center histidine 217 in D-amino acid oxidase by methyl-p-nitrobenzenesulfonate. The Journal of Biological Chemistry. 259: 5585-90. PMID 6143757 |
0.792 |
|
| 1984 |
Mayhew SG, Doherty G, McGRATH D, Williams CH. The pyruvate-oxidation system of the lipoamide dehydrogenase-containing anaerobe Peptococcus glycinophilus Biochemical Society Transactions. 12: 464-465. DOI: 10.1042/Bst0120464 |
0.325 |
|
| 1983 |
O'Donnell ME, Johnson FA, Williams CH. Proton nuclear magnetic resonance investigation of the mechanism of flavin C-4a adduct formation induced by oxidized nicotinamide adenine dinucleotide binding to monoalkylated pig heart lipoamide dehydrogenase. Biochemistry. 22: 3792-6. PMID 6688532 DOI: 10.1021/Bi00285A012 |
0.534 |
|
| 1983 |
O'Donnell ME, Williams CH. Proton stoichiometry in the reduction of the FAD and disulfide of Escherichia coli thioredoxin reductase. Evidence for a base at the active site. The Journal of Biological Chemistry. 258: 13795-805. PMID 6358211 |
0.518 |
|
| 1983 |
Swenson RP, Williams CH, Massey V. Identification of the histidine residue in D-amino acid oxidase that is covalently modified during inactivation by 5-dimethylaminonaphthalene-1-sulfonyl chloride. The Journal of Biological Chemistry. 258: 497-502. PMID 6129252 |
0.786 |
|
| 1982 |
Slaughter SR, Williams CH, Hultquist DE. Demonstration that bovine erythrocyte cytochrome b5 is the hydrophilic segment of liver microsomal cytochrome b5 Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 705: 228-237. PMID 7115739 DOI: 10.1016/0167-4838(82)90182-0 |
0.372 |
|
| 1982 |
Ronchi S, Minchiotti L, Galliano M, Curti B, Swenson RP, Williams CH, Massey V. The primary structure of D-amino acid oxidase from pig kidney. II. Isolation and sequence of overlap peptides and the complete sequence. The Journal of Biological Chemistry. 257: 8824-34. PMID 6124543 |
0.77 |
|
| 1982 |
Swenson RP, Williams CH, Massey V, Ronchi S, Minchiotti L, Galliano M, Curti B. The primary structure of D-amino acid oxidase from pig kidney. I. Isolation and sequence of the tryptic peptides. The Journal of Biological Chemistry. 257: 8817-23. PMID 6124542 |
0.78 |
|
| 1982 |
Swenson RP, Williams CH, Massey V. Chemical modification of D-amino acid oxidase. Amino acid sequence of the tryptic peptides containing tyrosine and lysine residues modified by fluorodinitrobenzene. The Journal of Biological Chemistry. 257: 1937-44. PMID 6120171 |
0.804 |
|
| 1981 |
Arscott LD, Thorpe C, Williams CH. Glutathione reductase from yeast. Differential reactivity of the nascent thiols in two-electron reduced enzyme and properties of a monoalkylated derivative. Biochemistry. 20: 1513-20. PMID 7013796 DOI: 10.1021/bi00509a016 |
0.33 |
|
| 1981 |
Thorpe C, Williams CH. Lipoamide dehydrogenase from pig heart. Pyridine nucleotide induced changes in monoalkylated two-electron reduced enzyme Biochemistry. 20: 1507-1513. PMID 6894384 DOI: 10.1021/Bi00509A015 |
0.48 |
|
| 1980 |
Nishino T, Massey V, Williams CH. Chemical modifications of D-amino acid oxidase. Evidence for active site histidine, tyrosine, and arginine residues. The Journal of Biological Chemistry. 255: 3610-6. PMID 6102567 |
0.719 |
|
| 1980 |
French JS, Black SD, Williams CH, Coon MJ. Studies On The Association Of P-450 Lm2 With Nadph-Cytochrome P-450 Reductase And With Tryptic Peptides Derived From The Reductase Microsomes, Drug Oxidations and Chemical Carcinogenesis. 387-390. DOI: 10.1016/B978-0-12-187701-9.50077-2 |
0.393 |
|
| 1979 |
Thorpe C, Matthews RG, Williams CH. Acyl-coenzyme A dehydrogenase from pig kidney. Purification and properties. Biochemistry. 18: 331-7. PMID 570409 DOI: 10.1021/Bi00569A016 |
0.718 |
|
| 1979 |
Williams CH, Arscott LD, Matthews RG, Thorpe C, Wilkinson KD. Methodology employed for anaerobic spectrophotometric titrations and for computer-assisted data analysis. Methods in Enzymology. 62: 185-98. PMID 374972 DOI: 10.1016/0076-6879(79)62217-6 |
0.671 |
|
| 1979 |
Black SD, French JS, Williams CH, Coon MJ. Role of a hydrophobic polypeptide in the N-terminal region of NADPH-cytochrome P-450 reductase in complex formation with P-450lm Biochemical and Biophysical Research Communications. 91: 1528-1535. PMID 118758 DOI: 10.1016/0006-291X(79)91238-5 |
0.445 |
|
| 1979 |
Matthews RG, Ballou DP, Williams CH. Reactions of pig heart lipoamide dehydrogenase with pyridine nucleotides. Evidence for an effector role for bound oxidized pyridine nucleotide. The Journal of Biological Chemistry. 254: 4974-81. PMID 36378 |
0.645 |
|
| 1977 |
Matthews RG, Ballou DP, Thorpe C, Williams CH. Ion pair formation in pig heart lipoamide dehydrogenase: rationalization of pH profiles for reactivity of oxidized enzyme with dihydrolipoamide and 2-electron-reduced enzyme with lipoamide and iodoacetamide. The Journal of Biological Chemistry. 252: 3199-207. PMID 16887 |
0.7 |
|
| 1976 |
Matthews RG, Williams CH. Measurement of the oxidation-reduction potentials for two-electron and four-electron reduction of lipoamide dehydrogenase from pig heart. The Journal of Biological Chemistry. 251: 3956-64. PMID 6467 |
0.705 |
|
| 1974 |
Thorpe C, Williams CH. Effects of low concentrations of guanidine hydrochloride on pig heart lipoamide dehydrogenase Biochemistry. 13: 3263-3268. PMID 4858227 DOI: 10.1021/Bi00713A013 |
0.445 |
|
| 1974 |
Williams CH. Monoamine oxidase-I. Specificity of some substrates and inhibitors Biochemical Pharmacology. 23: 615-628. PMID 4822746 DOI: 10.1016/0006-2952(74)90626-1 |
0.301 |
|
| 1974 |
Matthews RG, Arscott LD, Williams CH. Isolation, characterization and partial sequencing of cystine and thiol peptides of pig heart lipoamide dehydrogenase. Biochimica Et Biophysica Acta. 370: 26-38. PMID 4609485 DOI: 10.1016/0005-2744(74)90028-X |
0.722 |
|
| 1974 |
Matthews RG, Williams CH. Identification of the thiol residues involved in modifications of pig heart lipoamide dehydrogenase by cupric ion and by iodoacetamide. Biochimica Et Biophysica Acta. 370: 39-48. PMID 4371848 DOI: 10.1016/0005-2744(74)90029-1 |
0.737 |
|
| 1971 |
Massey V, Williams CH, Palmer G. The presence of S degrees-containing impurities in commercial samples of oxidized glutathione and their catalytic effect on the reduction of cytochrome c. Biochemical and Biophysical Research Communications. 42: 730-8. PMID 5543955 DOI: 10.1016/0006-291X(71)90548-1 |
0.706 |
|
| 1969 |
Foust GP, Burleigh BD, Mayhew SG, Williams CH, Massey V. An anaerobic titration assembly for spectrophotometric use. Analytical Biochemistry. 27: 530-5. PMID 5767206 DOI: 10.1016/0003-2697(69)90066-9 |
0.546 |
|
| 1968 |
Zanetti G, Williams CH, Massey V. Influence of photoirradiation on the oxidation-reduction state of thioredoxin reductase. The Journal of Biological Chemistry. 243: 4013-9. PMID 4299099 |
0.583 |
|
| 1967 |
Masters BSS, Williams CH, Kamin H. [92] The preparation and properties of microsomal TPNH-cytochrome c reductase from pig liver Methods in Enzymology. 10: 565-573. DOI: 10.1016/0076-6879(67)10098-0 |
0.671 |
|
| 1965 |
MASTERS BS, KAMIN H, GIBSON QH, WILLIAMS CH. STUDIES ON THE MECHANISM OF MICROSOMAL TRIPHOSPHOPYRIDINE NUCLEOTIDE-CYTOCHROME C REDUCTASE. The Journal of Biological Chemistry. 240: 921-31. PMID 14275154 |
0.61 |
|
| 1965 |
Massey V, Williams CH. On the reaction mechanism of yeast glutathione reductase. The Journal of Biological Chemistry. 240: 4470-80. PMID 4378936 |
0.588 |
|
| 1965 |
Kamin H, Masters BS, Gibson QH, Williams CH. Microsomal TPNH-cytochrome c reductase. Federation Proceedings. 24: 1164-71. PMID 4378721 |
0.604 |
|
| 1962 |
WILLIAMS CH, KAMIN H. Microsomal triphosphopyridine nucleotide-cytochrome c reductase of liver. The Journal of Biological Chemistry. 237: 587-95. PMID 14007123 |
0.588 |
|
| 1959 |
WILLIAMS CH, GIBBS RH, KAMIN H. A microsomal TPNH-neotetrazolium diaphorase. Biochimica Et Biophysica Acta. 32: 568-9. PMID 13844826 DOI: 10.1016/0006-3002(59)90643-2 |
0.624 |
|
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