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Mechanism and structure of thioredoxin reductase from Escherichia coli

The FASEB journal, 1995-10, Vol.9 (13), p.1267-1276

Williams, Charles H.

1995

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Twists in Catalysis: Alternating Conformations of Escherichia coli Thioredoxin Reductase

Science (American Association for the Advancement of Science), 2000-08, Vol.289 (5482), p.1190-1194

2000

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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 (Easton), 2007-07, Vol.46 (26), p.7875-7885

2007

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Mechanism-Based Inactivation of Thioredoxin Reductase from Plasmodium falciparum by Mannich Bases. Implication for Cytotoxicity

Biochemistry (Easton), 2003-11, Vol.42 (45), p.13319-13330

2003

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Crystal structure of Escherichia coli thioredoxin reductase refined at 2 angstrom resolution. Implications for a large conformational change during catalysis

Journal of molecular biology, 1994-02, Vol.236 (3), p.800-816

1994

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Kinetic characterization of glutathione reductase from the malarial parasite Plasmodium falciparum. Comparison with the human enzyme

The Journal of biological chemistry, 2000-12, Vol.275 (48), p.37317-37323

2000

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Thioredoxin Reductase from Plasmodium falciparum: Evidence for Interaction between the C-Terminal Cysteine Residues and the Active Site Disulfide−Dithiol

Biochemistry (Easton), 1999-03, Vol.38 (10), p.3187-3196

1999

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Reductive Half-Reaction of Thioredoxin Reductase from Escherichia coli

Biochemistry (Easton), 1997-08, Vol.36 (31), p.9464-9477

1997

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A Stable Mixed Disulfide between Thioredoxin Reductase and Its Substrate, Thioredoxin: Preparation and Characterization

Biochemistry (Easton), 1996-04, Vol.35 (15), p.4812-4819

1996

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Convergent evolution of similar function in two structurally divergent enzymes

Nature (London), 1991-07, Vol.352 (6331), p.172-174

1991

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Reductive and Oxidative Half-Reactions of Glutathione Reductase from Escherichia coli

Biochemistry (Easton), 1994-11, Vol.33 (46), p.13888-13895

1994

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The Mechanism of High M sub(r) Thioredoxin Reductase from Drosophila melanogaster

The Journal of biological chemistry, 2003-08, Vol.278 (35), p.33020-33028

2003

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Enzyme-Monitored Turnover of Escherichia coli Thioredoxin Reductase: Insights for Catalysis

Biochemistry (Easton), 1996-04, Vol.35 (15), p.4704-4712

1996

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Mechanism of Reduction of Quinones by Trypanosoma congolense Trypanothione Reductase

Biochemistry (Easton), 1994-03, Vol.33 (9), p.2509-2515

1994

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Characterization of Lipoamide Dehydrogenase from Escherichia coli Lacking the Redox Active Disulfide: C44S and C49S

Biochemistry (Easton), 1995-09, Vol.34 (37), p.11757-11765

1995

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The Role of Glycine 99 in l-Lactate Monooxygenase from Mycobacterium smegmatis

The Journal of biological chemistry, 1997-10, Vol.272 (43), p.27065-27076

1997

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Site-directed Mutagenesis of Glycine 99 to Alanine in L-Lactate Monooxygenase from Mycobacterium smegmatis

The Journal of biological chemistry, 1996-07, Vol.271 (29), p.17226-17233

1996

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Thioredoxin Reductase−Thioredoxin Fusion Enzyme from Mycobacterium leprae: Comparison with the Separately Expressed Thioredoxin Reductase

Biochemistry (Easton), 1998-11, Vol.37 (46), p.16378-16389

1998

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Lipoamide Dehydrogenase from Escherichia coli Lacking the Redox Active Disulfide: C44S and C49S. Redox Properties of the FAD and Interactions with Pyridine Nucleotides

Biochemistry (Easton), 1995-09, Vol.34 (37), p.11766-11776

1995

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Lactate monooxygenase. II. Site-directed mutagenesis of the postulated active site base histidine 290

The Journal of biological chemistry, 1994-03, Vol.269 (11), p.7989-7993

1994

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Effect of Pyridine Nucleotide on the Oxidative Half-Reaction of Escherichia coli Thioredoxin Reductase

Biochemistry (Easton), 1995-03, Vol.34 (11), p.3670-3677

1995

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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 Glutamate

The Journal of biological chemistry, 1999-08, Vol.274 (32), p.22289-22295

1999

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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 (Easton), 1990-03, Vol.29 (11), p.2831-2841

1990

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Lactate monooxygenase. I. Expression of the mycobacterial gene in Escherichia coli and site-directed mutagenesis of lysine 266

The Journal of biological chemistry, 1994-03, Vol.269 (11), p.7982-7988

1994

Volltextzugriff (PDF)

Redox Potentials for Yeast, Escherichia coli and Human Glutathione Reductase Relative to the NAD super(+)/NADH Redox Couple: Enzyme Forms Active in Catalysis

Biochemistry (Easton), 1998-11, Vol.37 (44), p.15575-15582

1998

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Mechanism and structure of thioredoxin reductase from Escherichia coli

Twists in Catalysis: Alternating Conformations of Escherichia coli Thioredoxin Reductase

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

Mechanism-Based Inactivation of Thioredoxin Reductase from Plasmodium falciparum by Mannich Bases. Implication for Cytotoxicity

Crystal structure of Escherichia coli thioredoxin reductase refined at 2 angstrom resolution. Implications for a large conformational change during catalysis

Kinetic characterization of glutathione reductase from the malarial parasite Plasmodium falciparum. Comparison with the human enzyme

Thioredoxin Reductase from Plasmodium falciparum: Evidence for Interaction between the C-Terminal Cysteine Residues and the Active Site Disulfide−Dithiol

Reductive Half-Reaction of Thioredoxin Reductase from Escherichia coli

A Stable Mixed Disulfide between Thioredoxin Reductase and Its Substrate, Thioredoxin: Preparation and Characterization

Convergent evolution of similar function in two structurally divergent enzymes

Reductive and Oxidative Half-Reactions of Glutathione Reductase from Escherichia coli

The Mechanism of High M sub(r) Thioredoxin Reductase from Drosophila melanogaster

Enzyme-Monitored Turnover of Escherichia coli Thioredoxin Reductase: Insights for Catalysis

Mechanism of Reduction of Quinones by Trypanosoma congolense Trypanothione Reductase

Characterization of Lipoamide Dehydrogenase from Escherichia coli Lacking the Redox Active Disulfide: C44S and C49S

The Role of Glycine 99 in l-Lactate Monooxygenase from Mycobacterium smegmatis

Site-directed Mutagenesis of Glycine 99 to Alanine in L-Lactate Monooxygenase from Mycobacterium smegmatis

Thioredoxin Reductase−Thioredoxin Fusion Enzyme from Mycobacterium leprae: Comparison with the Separately Expressed Thioredoxin Reductase

Lipoamide Dehydrogenase from Escherichia coli Lacking the Redox Active Disulfide: C44S and C49S. Redox Properties of the FAD and Interactions with Pyridine Nucleotides

Lactate monooxygenase. II. Site-directed mutagenesis of the postulated active site base histidine 290

Effect of Pyridine Nucleotide on the Oxidative Half-Reaction of Escherichia coli Thioredoxin Reductase

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 Glutamate

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

Lactate monooxygenase. I. Expression of the mycobacterial gene in Escherichia coli and site-directed mutagenesis of lysine 266

Redox Potentials for Yeast, Escherichia coli and Human Glutathione Reductase Relative to the NAD super(+)/NADH Redox Couple: Enzyme Forms Active in Catalysis

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