(Q35813283)

10 August 2017

1 reference

title

Flavoprotein disulfide reductases: advances in chemistry and function (English)

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10 August 2017

Argyrides Argyrou

1

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ORCID Public Data File 2021

author name string

John S Blanchard

series ordinal

2

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10 August 2017

1 January 2004

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Progress in Molecular Biology and Translational Science

10 August 2017

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10 August 2017

78

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10 August 2017

89-142

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Expression, purification, and characterization of Mycobacterium tuberculosis mycothione reductase

10 August 2017

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Thioredoxin reductase two modes of catalysis have evolved

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

AhpF and other NADH:peroxiredoxin oxidoreductases, homologues of low Mr thioredoxin reductase

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Structural, redox, and mechanistic parameters for cysteine-sulfenic acid function in catalysis and regulation

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Coenzyme A disulfide reductase, the primary low molecular weight disulfide reductase from Staphylococcus aureus. Purification and characterization of the native enzyme

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Aliphatic epoxide carboxylation

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Microbial metabolism of aliphatic alkenes

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

The structure of the flavoenzyme glutathione reductase

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

X-ray structure of lipoamide dehydrogenase from Azotobacter vinelandii determined by a combination of molecular and isomorphous replacement techniques

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

X-ray structure of trypanothione reductase from Crithidia fasciculata at 2.4-A resolution

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Kinetics and crystallographic analysis of human glutathione reductase in complex with a xanthene inhibitor

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

The refined crystal structure of Pseudomonas putida lipoamide dehydrogenase complexed with NAD+ at 2.45 A resolution

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

The structure of Trypanosoma cruzi trypanothione reductase in the oxidized and NADPH reduced state

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Characterization of lipoamide dehydrogenase from Escherichia coli lacking the redox active disulfide: C44S and C49S.

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Lipoamide dehydrogenase from Escherichia coli lacking the redox active disulfide: C44S and C49S. Redox properties of the FAD and interactions with pyridine nucleotides

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Site-directed mutagenesis of the redox-active cysteines of Trypanosoma cruzi trypanothione reductase.

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Directed mutagenesis of the redox-active disulphide bridge in glutathione reductase from Escherichia coli.

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Glutathione reductase from yeast. Differential reactivity of the nascent thiols in two-electron reduced enzyme and properties of a monoalkylated derivative.

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Lipoamide dehydrogenase from pig heart. Pyridine nucleotide induced changes in monoalkylated two-electron reduced enzyme

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Lipoamide dehydrogenase from Azotobacter vinelandii: site-directed mutagenesis of the His450-Glu455 diad. Kinetics of wild-type and mutated enzymes

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Reductive and oxidative half-reactions of glutathione reductase from Escherichia coli.

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Catalysis of diaphorase reactions by Mycobacterium tuberculosis lipoamide dehydrogenase occurs at the EH4 level

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Mycobacterium tuberculosis lipoamide dehydrogenase is encoded by Rv0462 and not by the lpdA or lpdB genes

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Kinetic isotope effect analysis of the reaction catalyzed by Trypanosoma congolense trypanothione reductase

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Kinetic studies of multifunctional reactions catalysed by lipoamide dehydrogenase.

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

pH dependent kinetic studies of lipoamide dehydrogenase catalysis

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

A branching reaction mechanism of glutathione reductase

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

A 'branched' mechanism of the reverse reaction of yeast glutathione reductase. An estimation of the enzyme standard potential values from the steady-state kinetics data

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Switching kinetic mechanism and putative proton donor by directed mutagenesis of glutathione reductase.

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Cooperativity induced by a single mutation at the subunit interface of a dimeric enzyme: glutathione reductase

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Altering kinetic mechanism and enzyme stability by mutagenesis of the dimer interface of glutathione reductase

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

A lipoamide dehydrogenase from Neisseria meningitidis has a lipoyl domain

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Sequence and organization of genes encoding enzymes involved in pyruvate metabolism in Mycoplasma capricolum

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Biochemical and molecular characterization of the Alcaligenes eutrophus pyruvate dehydrogenase complex and identification of a new type of dihydrolipoamide dehydrogenase

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Biochemical and molecular characterization of the Clostridium magnum acetoin dehydrogenase enzyme system

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Interaction between the lipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system. 1. Biochemical studies

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Intermediates in the catalytic action of lipoyl dehydrogenase (diaphorase)

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

The lipoamide dehydrogenase from Mycobacterium tuberculosis permits the direct observation of flavin intermediates in catalysis

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Properties of lipoamide dehydrogenase altered by site-directed mutagenesis at a key residue (Il84Y) in the pyridine nucleotide binding domain

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Modulation of the oxidation-reduction potential of the flavin in lipoamide dehydrogenase from Escherichia coli by alteration of a nearby charged residue, K53R.

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Lipoamide dehydrogenase from Azotobacter vinelandii. The role of the C-terminus in catalysis and dimer stabilization

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Lipoamide dehydrogenase from Azotobacter vinelandii: site-directed mutagenesis of the His450-Glu455 diad. Spectral properties of wild type and mutated enzymes

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

The interaction between lipoamide dehydrogenase and the peripheral-component-binding domain from the Azotobacter vinelandii pyruvate dehydrogenase complex

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Inhibition of lipoyl dehydrogenase by trace metals

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Isolation and properties of a flavoprotein from heart muscle tissue

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

On the catalytic function of heart flavoprotein

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

The identity of diaphorase and lipoyl dehydrogenase

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

The identity of diaphorase and lipoic dehydrogenase

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

The mechanism of the quinone reductase reaction of pig heart lipoamide dehydrogenase

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Ubiquinone is reduced by lipoamide dehydrogenase and this reaction is potently stimulated by zinc

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Reduction of ubiquinone by lipoamide dehydrogenase

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

The conformational stability of the redox states of lipoamide dehydrogenase from Azotobacter vinelandii

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Dihydrolipoamide dehydrogenase: a 'new' function for an old enzyme?

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Dihydrolipoamide dehydrogenase from Trypanosoma brucei. Characterization and cellular location

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Structure, catalytic mechanism, and evolution of the glutathione transferases

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

[5] Diversity of glutathione peroxidases

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Refined structure of glutathione reductase at 1.54 A resolution

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Crystallographic analysis of the binding of NADPH, NADPH fragments, and NADPH analogues to glutathione reductase

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Substrate binding and catalysis by glutathione reductase as derived from refined enzyme: substrate crystal structures at 2 A resolution

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Glutathione reductase: solvent equilibrium and kinetic isotope effects

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Role of active site tyrosine residues in catalysis by human glutathione reductase

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

One- and two-electron reduction of quinones by glutathione reductase

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Mechanism of reduction of quinones by Trypanosoma congolense trypanothione reductase

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Inhibition of human glutathione reductase by the nitrosourea drugs 1,3-bis(2-chloroethyl)-1-nitrosourea and 1-(2-chloroethyl)-3-(2-hydroxyethyl)-1-nitrosourea. A crystallographic analysis

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Ajoene is an inhibitor and subversive substrate of human glutathione reductase and Trypanosoma cruzi trypanothione reductase: crystallographic, kinetic, and spectroscopic studies

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Disulfide-Reductase Inhibitors as Chemotherapeutic Agents: The Design of Drugs for Trypanosomiasis and Malaria

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Enzyme inactivation through sulfhydryl oxidation by physiologic NO-carriers

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Crystal structure of the antioxidant enzyme glutathione reductase inactivated by peroxynitrite

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Inhibition of human glutathione reductase by 10-arylisoalloxazines: crystalline, kinetic, and electrochemical studies

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

A crystallographic study of the glutathione binding site of glutathione reductase at 0.3-nm resolution

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Glutathione reductase of the malarial parasite Plasmodium falciparum: crystal structure and inhibitor development

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Recombinant Plasmodium falciparum glutathione reductase is inhibited by the antimalarial dye methylene blue

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Antimalarial dyes revisited: xanthenes, azines, oxazines, and thiazines

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Trypanothione: a novel bis(glutathionyl)spermidine cofactor for glutathione reductase in trypanosomatids

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Tryparedoxin and tryparedoxin peroxidase

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Trypanothione-dependent synthesis of deoxyribonucleotides by Trypanosoma brucei ribonucleotide reductase

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Disruption of the trypanothione reductase gene of Leishmania decreases its ability to survive oxidative stress in macrophages.

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Evidence that trypanothione reductase is an essential enzyme in Leishmania by targeted replacement of the tryA gene locus

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Trypanosomes lacking trypanothione reductase are avirulent and show increased sensitivity to oxidative stress

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Down-regulation of Leishmania donovani trypanothione reductase by heterologous expression of a trans-dominant mutant homologue: effect on parasite intracellular survival

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Crystal structure of Trypanosoma cruzi trypanothione reductase in complex with trypanothione, and the structure-based discovery of new natural product inhibitors

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Glutathione reductase turned into trypanothione reductase: structural analysis of an engineered change in substrate specificity

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Mutational analysis of parasite trypanothione reductase: acquisition of glutathione reductase activity in a triple mutant

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Redox enzyme engineering: conversion of human glutathione reductase into a trypanothione reductase

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Engineering the substrate specificity of glutathione reductase toward that of trypanothione reduction

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Parasite-specific trypanothione reductase as a drug target molecule

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Trypanothione reductase from Trypanosoma cruzi. Catalytic properties of the enzyme and inhibition studies with trypanocidal compounds

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

(2,2':6',2"-Terpyridine)platinum(II) complexes are irreversible inhibitors of Trypanosoma cruzi trypanothione reductase but not of human glutathione reductase

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Crystal structure of the Trypanosoma cruzi trypanothione reductase.mepacrine complex

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Optimising inhibitors of trypanothione reductase using solid-phase chemistry

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

"Subversive" substrates for the enzyme trypanothione disulfide reductase: alternative approach to chemotherapy of Chagas disease

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Chinifur, a selective inhibitor and "subversive substrate" for Trypanosoma congolense trypanothione reductase

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

2- and 3-substituted 1,4-naphthoquinone derivatives as subversive substrates of trypanothione reductase and lipoamide dehydrogenase from Trypanosoma cruzi: synthesis and correlation between redox cycling activities and in vitro cytotoxicity.

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Structure of a novel disulfide of 2-(N-acetylcysteinyl)amido-2-deoxy-alpha-D-glucopyranosyl-myo-inositol produced by Streptomyces sp

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Thiols of intracellular pathogens. Identification of ovothiol A in Leishmania donovani and structural analysis of a novel thiol from Mycobacterium bovis

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Distribution of thiols in microorganisms: mycothiol is a major thiol in most actinomycetes

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

ATP-dependent L-cysteine:1D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase, mycothiol biosynthesis enzyme MshC, is related to class I cysteinyl-tRNA synthetases

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

The glycosyltransferase gene encoding the enzyme catalyzing the first step of mycothiol biosynthesis (mshA)

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Mycothiol biochemistry

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

The metabolism of nitrosothiols in the Mycobacteria: identification and characterization of S-nitrosomycothiol reductase

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Mycobacterium tuberculosis mycothione reductase: pH dependence of the kinetic parameters and kinetic isotope effects

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Organization, expression, and evolution of genes for mercury resistance

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Structure of the detoxification catalyst mercuric ion reductase from Bacillus sp. strain RC607

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Deoxyribonucleic acid sequence of a gene from the Pseudomonas transposon TN501 encoding mercuric reductase

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Mutagenesis of the N- and C-terminal cysteine pairs of Tn501 mercuric ion reductase: consequences for bacterial detoxification of mercurials

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

C-terminal cysteines of Tn501 mercuric ion reductase

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Rapid reduction of Hg(II) by mercuric ion reductase does not require the conserved C-terminal cysteine pair using HgBr2 as the substrate

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Alternative routes for entry of HgX2 into the active site of mercuric ion reductase depend on the nature of the X ligands

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Plasmid-mediated heavy metal resistances

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Cloning and expression in Escherichia coli of chromosomal mercury resistance genes from a Bacillus sp

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Mercuric reductase: homology to glutathione reductase and lipoamide dehydrogenase. Iodoacetamide alkylation and sequence of the active site peptide

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Evidence for the participation of Cys558 and Cys559 at the active site of mercuric reductase

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Directed mutagenesis of the redox-active disulfide in the flavoenzyme mercuric ion reductase

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Mutagenesis of the redox-active disulfide in mercuric ion reductase: catalysis by mutant enzymes restricted to flavin redox chemistry

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Rapid-scan stopped-flow studies of the pH dependence of the reaction between mercuric reductase and NADPH

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

In vivo and in vitro effects of mutagenesis of active site tyrosine residues of mercuric reductase

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Role of tyrosine residues in Hg(II) detoxification by mercuric reductase from Bacillus sp. strain RC607

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Communication between the active sites in dimeric mercuric ion reductase: an alternating sites hypothesis for catalysis

1 reference

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7 January 2021

Physiological functions of thioredoxin and thioredoxin reductase

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Three-dimensional structure of a mammalian thioredoxin reductase: implications for mechanism and evolution of a selenocysteine-dependent enzyme

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Regulation of human thioredoxin reductase expression and activity by 3'-untranslated region selenocysteine insertion sequence and mRNA instability elements

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

The role of the C-terminus for catalysis of the large thioredoxin reductase from Plasmodium falciparum

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

The mechanism of high Mr thioredoxin reductase from Drosophila melanogaster

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Substitution of the thioredoxin system for glutathione reductase in Drosophila melanogaster

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Selenoprotein oxidoreductase with specificity for thioredoxin and glutathione systems

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

The disulfide redox system of Schistosoma mansoni and the importance of a multifunctional enzyme, thioredoxin glutathione reductase

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Structure and mechanism of mammalian thioredoxin reductase: the active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Thioredoxin reductase from Plasmodium falciparum: evidence for interaction between the C-terminal cysteine residues and the active site disulfide-dithiol

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Human thioredoxin reductase from HeLa cells: selective alkylation of selenocysteine in the protein inhibits enzyme activity and reduction with NADPH influences affinity to heparin

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Mammalian thioredoxin reductase is irreversibly inhibited by dinitrohalobenzenes by alkylation of both the redox active selenocysteine and its neighboring cysteine residue

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

1-Chloro-2,4-dinitrobenzene is an irreversible inhibitor of human thioredoxin reductase. Loss of thioredoxin disulfide reductase activity is accompanied by a large increase in NADPH oxidase activity

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Human placenta thioredoxin reductase. Isolation of the selenoenzyme, steady state kinetics, and inhibition by therapeutic gold compounds

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Mechanism and structure of thioredoxin reductase from Escherichia coli

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

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 flavi

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Potential active-site base of thioredoxin reductase from Escherichia coli: examination of histidine245 and aspartate139 by site-directed mutagenesis.

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Convergent evolution of similar function in two structurally divergent enzymes

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

A stable mixed disulfide between thioredoxin reductase and its substrate, thioredoxin: preparation and characterization

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Reductive half-reaction of thioredoxin reductase from Escherichia coli

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Thioredoxin reductase from Escherichia coli: evidence of restriction to a single conformation upon formation of a crosslink between engineered cysteines

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Enzyme-monitored turnover of Escherichia coli thioredoxin reductase: insights for catalysis

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

1 reference

7 January 2021

Structure, mechanism and regulation of peroxiredoxins

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 2. Cystine disulfides involved in catalysis of peroxide reduction

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Requirement for the two AhpF cystine disulfide centers in catalysis of peroxide reduction by alkyl hydroperoxide reductase.

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

AhpF can be dissected into two functional units: tandem repeats of two thioredoxin-like folds in the N-terminus mediate electron transfer from the thioredoxin reductase-like C-terminus to AhpC.

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Role of cysteine 337 and cysteine 340 in flavoprotein that functions as NADH oxidase from Amphibacillus xylanus studied by site-directed mutagenesis

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Activity of one of two engineered heterodimers of AhpF, the NADH:peroxiredoxin oxidoreductase from Salmonella typhimurium, reveals intrasubunit electron transfer between domains

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Attachment of the N-terminal domain of Salmonella typhimurium AhpF to Escherichia coli thioredoxin reductase confers AhpC reductase activity but does not affect thioredoxin reductase activity.

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Thioredoxin reductase-thioredoxin fusion enzyme from Mycobacterium leprae: comparison with the separately expressed thioredoxin reductase

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Reaction mechanism of Amphibacillus xylanus NADH oxidase/alkyl hydroperoxide reductase flavoprotein.

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Structure of intact AhpF reveals a mirrored thioredoxin-like active site and implies large domain rotations during catalysis

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Roles for the two cysteine residues of AhpC in catalysis of peroxide reduction by alkyl hydroperoxide reductase from Salmonella typhimurium.

1 reference

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7 January 2021

Novel application of 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole to identify cysteine sulfenic acid in the AhpC component of alkyl hydroperoxide reductase.

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Staphylococcus aureus coenzyme A disulfide reductase, a new subfamily of pyridine nucleotide-disulfide oxidoreductase. Sequence, expression, and analysis of cdr.

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Cloning, sequence and overexpression of NADH peroxidase from Streptococcus faecalis 10C1. Structural relationship with the flavoprotein disulfide reductases.

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Molecular cloning and analysis of the gene encoding the NADH oxidase from Streptococcus faecalis 10C1. Comparison with NADH peroxidase and the flavoprotein disulfide reductases

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Coenzyme A-disulfide reductase from Staphylococcus aureus: evidence for asymmetric behavior on interaction with pyridine nucleotides

1 reference

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7 January 2021

Structure of the native cysteine-sulfenic acid redox center of enterococcal NADH peroxidase refined at 2.8 A resolution

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

The structure of NADH peroxidase from Streptococcus faecalis at 3.3 A resolution

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

NADH binding site and catalysis of NADH peroxidase

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

An L40C mutation converts the cysteine-sulfenic acid redox center in enterococcal NADH peroxidase to a disulfide

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Crystallographic analyses of NADH peroxidase Cys42Ala and Cys42Ser mutants: active site structures, mechanistic implications, and an unusual environment of Arg 303

1 reference

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7 January 2021

Analysis of the kinetic and redox properties of the NADH peroxidase R303M mutant: correlation with the crystal structure

1 reference

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7 January 2021

Analysis of the kinetic and redox properties of NADH peroxidase C42S and C42A mutants lacking the cysteine-sulfenic acid redox center

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Analysis of the kinetic mechanism of enterococcal NADH peroxidase reveals catalytic roles for NADH complexes with both oxidized and two-electron-reduced enzyme forms

1 reference

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7 January 2021

Chemical mechanism and rate-limiting steps in the reaction catalyzed by Streptococcus faecalis NADH peroxidase

1 reference

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7 January 2021

The active-site histidine-10 of enterococcal NADH peroxidase is not essential for catalytic activity

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Contribution of NADH oxidase to aerobic metabolism of Streptococcus pyogenes

1 reference

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7 January 2021

Equilibrium analyses of the active-site asymmetry in enterococcal NADH oxidase: role of the cysteine-sulfenic acid redox center

1 reference

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7 January 2021

Oxygen reactivity of an NADH oxidase C42S mutant: evidence for a C(4a)-peroxyflavin intermediate and a rate-limiting conformational change.

1 reference

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7 January 2021

Identification and characterization of epoxide carboxylase activity in cell extracts of Nocardia corallina B276.

1 reference

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7 January 2021

Microbial metabolism of short-chain unsaturated hydrocarbons

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7 January 2021

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

1 reference

7 January 2021

Unusual coenzymes of methanogenesis

1 reference

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7 January 2021

A role for coenzyme M (2-mercaptoethanesulfonic acid) in a bacterial pathway of aliphatic epoxide carboxylation

1 reference

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7 January 2021

Evidence that a linear megaplasmid encodes enzymes of aliphatic alkene and epoxide metabolism and coenzyme M (2-mercaptoethanesulfonate) biosynthesis in Xanthobacter strain Py2

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Structural basis for CO2 fixation by a novel member of the disulfide oxidoreductase family of enzymes, 2-ketopropyl-coenzyme M oxidoreductase/carboxylase

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

A novel type of pyridine nucleotide-disulfide oxidoreductase is essential for NAD+- and NADPH-dependent degradation of epoxyalkanes by Xanthobacter strain Py2.

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Purification and characterization of a flavoprotein involved in the degradation of epoxyalkanes by Xanthobacter Py2

1 reference

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7 January 2021

Characterization of five catalytic activities associated with the NADPH:2-ketopropyl-coenzyme M [2-(2-ketopropylthio)ethanesulfonate] oxidoreductase/carboxylase of the Xanthobacter strain Py2 epoxide carboxylase system

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Carbon dioxide fixation in the metabolism of propylene and propylene oxide by Xanthobacter strain Py2.

1 reference

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7 January 2021

Carboxylation of epoxides to beta-keto acids in cell extracts of Xanthobacter strain Py2.

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Proton translocation by transhydrogenase

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Cloning, sequence, and properties of the soluble pyridine nucleotide transhydrogenase of Pseudomonas fluorescens

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

The udhA gene of Escherichia coli encodes a soluble pyridine nucleotide transhydrogenase.

1 reference

https://api.crossref.org/works/10.1016%2FS0079-6603%2804%2978003-4

7 January 2021

Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence

1 reference

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7 January 2021

10.1016/S0079-6603(04)78003-4

Identifiers

DOI

1 reference

10 August 2017

1 reference

PubMed ID

15210329