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Charles Williams

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Zhiyong Cheng; David P Ballou; Jinfeng Zhang; Charles H Williams
Reactivity of thioredoxin as a protein thiol-disulfide oxidoreductase.
Hsin-Hung Huang; L David Arscott; David P Ballou; Charles H Williams
Function of Glu-469' in the acid-base catalysis of thioredoxin reductase from Drosophila melanogaster.
Hsin-Hung Huang; L David Arscott; David P Ballou; Charles H Williams
Acid-base catalysis in the mechanism of thioredoxin reductase from Drosophila melanogaster.

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All Publications

2011: Zhiyong Cheng; David P Ballou; Jinfeng Zhang; Charles H Williams
Reactivity of thioredoxin as a protein thiol-disulfide oxidoreductase.
Chemical reviews 2011;111(9):5768-83.
2008: Hsin-Hung Huang; L David Arscott; David P Ballou; Charles H Williams
Function of Glu-469' in the acid-base catalysis of thioredoxin reductase from Drosophila melanogaster.
Biochemistry 2008;47(48):12769-76.
2008: Hsin-Hung Huang; L David Arscott; David P Ballou; Charles H Williams
Acid-base catalysis in the mechanism of thioredoxin reductase from Drosophila melanogaster.
Biochemistry 2008;47(6):1721-31.
2007: Zhiyong Cheng; L David Arscott; David P Ballou; Charles H Williams
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 2007;46(26):7875-85.
2006: Paul J McMillan; L David Arscott; David P Ballou; Katja Becker; Charles H Williams; Sylke Müller
Identification of acid-base catalytic residues of high-Mr thioredoxin reductase from Plasmodium falciparum.
The Journal of biological chemistry 2006;281(44):32967-77.
2006: Linda Johansson; L David Arscott; David P Ballou; Charles H Williams; Elias Arnér
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 2006;41(4):649-56.
2006: Adriano D Andricopulo; M B Akoachere; R Krogh; C Nickel; Michael McLeish; George L Kenyon; L David Arscott; Charles H Williams; Elisabeth Davioud; Katja Becker
Specific inhibitors of Plasmodium falciparum thioredoxin reductase as potential antimalarial agents.
Bioorganic & medicinal chemistry letters 2006;16(8):2283-92.
2005: Marcel Deponte; Sabine Urig; L David Arscott; Karin Fritz-Wolf; Régis Réau; Christel Herold-Mende; Sasa Koncarevic; Markus Meyer; Elisabeth Davioud; David P Ballou; Charles H Williams; Katja Becker
Mechanistic studies on a novel, highly potent gold-phosphole inhibitor of human glutathione reductase.
The Journal of biological chemistry 2005;280(21):20628-37.
2004: Wolfgang Eisenreich; Kristina Kemter; Adelbert Bacher; Scott B Mulrooney; Charles H Williams; Franz Müller
13C-, 15N- and 31P-NMR studies of oxidized and reduced low molecular mass thioredoxin reductase and some mutant proteins.
European journal of biochemistry / FEBS 2004;271(8):1437-52.
2003: Elisabeth Davioud; Michael McLeish; Donna M Veine; David Giegel; L David Arscott; Adriano D Andricopulo; Katja Becker; Sylke Müller; R Heiner Schirmer; Charles H Williams; George L Kenyon
Mechanism-based inactivation of thioredoxin reductase from Plasmodium falciparum by Mannich bases. Implication for cytotoxicity.
Biochemistry 2003;42(45):13319-30.
2003: Stephan Gromer; Linda Johansson; Holger Bauer; L David Arscott; Susanne Rauch; David P Ballou; Charles H Williams; R Heiner Schirmer; Elias Arnér
Active sites of thioredoxin reductases: why selenoproteins?
Proceedings of the National Academy of Sciences of the United States of America 2003;100(22):12618-23.
2003: Holger Bauer; Vincent Massey; L David Arscott; R Heiner Schirmer; David P Ballou; Charles H Williams
The mechanism of high Mr thioredoxin reductase from Drosophila melanogaster.
The Journal of biological chemistry 2003;278(35):33020-8.
2001: Petra A W van den Berg; Scott B Mulrooney; Bas Gobets; Ivo H M van Stokkum; Arie van Hoek; Charles H Williams; Antonie J W G Visser
Exploring the conformational equilibrium of E. coli thioredoxin reductase: characterization of two catalytically important states by ultrafast flavin fluorescence spectroscopy.
Protein science : a publication of the Protein Society 2001;10(10):2037-49.
2000: C C Bohme; L David Arscott; Katja Becker; R Heiner Schirmer; Charles H Williams
Kinetic characterization of glutathione reductase from the malarial parasite Plasmodium falciparum. Comparison with the human enzyme.
The Journal of biological chemistry 2000;275(48):37317-23.
2000: Charles H Williams; L David Arscott; Sylke Müller; Brett W Lennon; Martha L Ludwig; Pan-Fen Wang; Donna M Veine; Katja Becker; R Heiner Schirmer
Thioredoxin reductase two modes of catalysis have evolved.
European journal of biochemistry / FEBS 2000;267(20):6110-7.
2000: Charles H Williams
Thioredoxin-thioredoxin reductase--a system that has come of age.
European journal of biochemistry / FEBS 2000;267(20):6101.
2000: Brett W Lennon; Charles H Williams; Martha L Ludwig
Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase.
Science (New York, N.Y.) 2000;289(5482):1190-4.
2000: L David Arscott; Donna M Veine; Charles H Williams
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 2000;39(16):4711-21.
1999: Brett W Lennon; Charles H Williams; Martha L Ludwig
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 1999;8(11):2366-79.
1999: SA Sanders; Charles H Williams; Vincent Massey
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 1999;274(32):22289-95.
1999: Pan-Fen Wang; L David Arscott; T W Gilberger; Sylke Müller; Charles H Williams
Thioredoxin reductase from Plasmodium falciparum: evidence for interaction between the C-terminal cysteine residues and the active site disulfide-dithiol.
Biochemistry 1999;38(10):3187-96.
1998: Pan-Fen Wang; JA Marcinkeviciene; Charles H Williams; John S Blanchard
Thioredoxin reductase-thioredoxin fusion enzyme from Mycobacterium leprae: comparison with the separately expressed thioredoxin reductase.
Biochemistry 1998;37(46):16378-89.
1998: Donna M Veine; L David Arscott; Charles H Williams
Redox potentials for yeast, Escherichia coli and human glutathione reductase relative to the NAD+/NADH redox couple: enzyme forms active in catalysis.
Biochemistry 1998;37(44):15575-82.
1998: R Luise Krauth-Siegel; L David Arscott; A Schönleben-Janas; R Heiner Schirmer; Charles H Williams
Role of active site tyrosine residues in catalysis by human glutathione reductase.
Biochemistry 1998;37(40):13968-77.
1998: Stephan Gromer; L David Arscott; Charles H Williams; R Heiner Schirmer; Katja Becker
Human placenta thioredoxin reductase. Isolation of the selenoenzyme, steady state kinetics, and inhibition by therapeutic gold compounds.
The Journal of biological chemistry 1998;273(32):20096-101.
1998: Donna M Veine; Scott B Mulrooney; Pan-Fen Wang; Charles H Williams
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 1998;7(6):1441-50.
1998: P M Färber; L David Arscott; Charles H Williams; Katja Becker; R Heiner Schirmer
Recombinant Plasmodium falciparum glutathione reductase is inhibited by the antimalarial dye methylene blue.
FEBS letters 1998;422(3):311-4.
1998: Donna M Veine; K Ohnishi; Charles H Williams
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 1998;7(2):369-75.
1997: W Sun; Charles H Williams; Vincent Massey
The role of glycine 99 in L-lactate monooxygenase from Mycobacterium smegmatis.
The Journal of biological chemistry 1997;272(43):27065-76.
1997: Scott B Mulrooney; Charles H Williams
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 1997;6(10):2188-95.
1997: Brett W Lennon; Charles H Williams
Reductive half-reaction of thioredoxin reductase from Escherichia coli.
Biochemistry 1997;36(31):9464-77.
1997: L David Arscott; Stephan Gromer; R Heiner Schirmer; Katja Becker; Charles H Williams
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 1997;94(8):3621-6.
1996: W Sun; Charles H Williams; Vincent Massey
Site-directed mutagenesis of glycine 99 to alanine in L-lactate monooxygenase from Mycobacterium smegmatis.
The Journal of biological chemistry 1996;271(29):17226-33.
1996: P F Wang; Donna M Veine; S H Ahn; Charles H Williams
A stable mixed disulfide between thioredoxin reductase and its substrate, thioredoxin: preparation and characterization.
Biochemistry 1996;35(15):4812-9.
1996: Brett W Lennon; Charles H Williams
Enzyme-monitored turnover of Escherichia coli thioredoxin reductase: insights for catalysis.
Biochemistry 1996;35(15):4704-12.
1995: Charles H Williams
Mechanism and structure of thioredoxin reductase from Escherichia coli.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology 1995;9(13):1267-76.
1995: N Hopkins; Charles H Williams
Lipoamide dehydrogenase from Escherichia coli lacking the redox active disulfide: C44S and C49S. Redox properties of the FAD and interactions with pyridine nucleotides.
Biochemistry 1995;34(37):11766-76.
1995: N Hopkins; Charles H Williams
Characterization of lipoamide dehydrogenase from Escherichia coli lacking the redox active disulfide: C44S and C49S.
Biochemistry 1995;34(37):11757-65.
1995: Brett W Lennon; Charles H Williams
Effect of pyridine nucleotide on the oxidative half-reaction of Escherichia coli thioredoxin reductase.
Biochemistry 1995;34(11):3670-7.
1994: P Rietveld; L David Arscott; A Berry; Nigel S Scrutton; M P Deonarain; Richard N Perham; Charles H Williams
Reductive and oxidative half-reactions of glutathione reductase from Escherichia coli.
Biochemistry 1994;33(46):13888-95.
1994: K Maeda-Yorita; George Russell; J R Guest; Vincent Massey; Charles H Williams
Modulation of the oxidation-reduction potential of the flavin in lipoamide dehydrogenase from Escherichia coli by alteration of a nearby charged residue, K53R.
Biochemistry 1994;33(20):6213-20.
1994: Scott B Mulrooney; Charles H Williams
Potential active-site base of thioredoxin reductase from Escherichia coli: examination of histidine245 and aspartate139 by site-directed mutagenesis.
Biochemistry 1994;33(11):3148-54.
1994: U Müh; Charles H Williams; Vincent Massey
Lactate monooxygenase. III. Additive contributions of active site residues to catalytic efficiency and stabilization of an anionic transition state.
The Journal of biological chemistry 1994;269(11):7994-8000.
1994: U Müh; Charles H Williams; Vincent Massey
Lactate monooxygenase. II. Site-directed mutagenesis of the postulated active site base histidine 290.
The Journal of biological chemistry 1994;269(11):7989-93.
1994: U Müh; Vincent Massey; Charles H Williams
Lactate monooxygenase. I. Expression of the mycobacterial gene in Escherichia coli and site-directed mutagenesis of lysine 266.
The Journal of biological chemistry 1994;269(11):7982-8.
1992: Andrew Prongay; Charles H Williams
Oxidation-reduction properties of Escherichia coli thioredoxin reductase altered at each active site cysteine residue.
The Journal of biological chemistry 1992;267(35):25181-8.
1992: Peter Macheroux; Scott B Mulrooney; Charles H Williams; Vincent Massey
Direct expression of active spinach glycolate oxidase in Escherichia coli.
Biochimica et biophysica acta 1992;1132(1):11-6.
1991: K Maeda-Yorita; George Russell; J R Guest; Vincent Massey; Charles H Williams
Properties of lipoamide dehydrogenase altered by site-directed mutagenesis at a key residue (I184Y) in the pyridine nucleotide binding domain.
Biochemistry 1991;30(51):11788-95.
1991: Susan Miller; Vincent Massey; Charles H Williams; David P Ballou; Christopher T Walsh
Communication between the active sites in dimeric mercuric ion reductase: an alternating sites hypothesis for catalysis.
Biochemistry 1991;30(10):2600-12.
1990: Andrew Prongay; Charles H Williams
Evidence for direct interaction between cysteine 138 and the flavin in thioredoxin reductase. A study using flavin analogs.
The Journal of biological chemistry 1990;265(31):18968-75.
1990: D A Giegel; Charles H Williams; Vincent Massey
L-lactate 2-monooxygenase from Mycobacterium smegmatis. Cloning, nucleotide sequence, and primary structure homology within an enzyme family.
The Journal of biological chemistry 1990;265(12):6626-32.
1990: Susan Miller; Vincent Massey; David P Ballou; Charles H Williams; M D Distefano; M J Moore; Christopher T Walsh
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 1990;29(11):2831-41.
1989: Andrew Prongay; David R Engelke; Charles H Williams
Characterization of two active site mutations of thioredoxin reductase from Escherichia coli.
The Journal of biological chemistry 1989;264(5):2656-64.
1989: Susan Miller; M J Moore; Vincent Massey; Charles H Williams; M D Distefano; David P Ballou; Christopher T Walsh
Evidence for the participation of Cys558 and Cys559 at the active site of mercuric reductase.
Biochemistry 1989;28(3):1194-205.
1988: A Negri; Vincent Massey; Charles H Williams; L M Schopfer
The kinetic mechanism of beef kidney D-aspartate oxidase.
The Journal of biological chemistry 1988;263(27):13557-63.