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Volumn 40, Issue 13, 2001, Pages 3912-3919
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Activity of one of two engineered heterodimers of AhpF, the NADH: Peroxiredoxin oxidoreductase from Salmonella typhimurium, reveals intrasubunit electron transfer between domains
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Author keywords
[No Author keywords available]
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Indexed keywords
INTRASUBUNIT PROCESS;
CATALYSIS;
CHARGE TRANSFER;
CHEMICAL BONDS;
ENZYME KINETICS;
MONOMERS;
REDOX REACTIONS;
REDUCTION;
DIMERS;
CYSTEINE;
DIMER;
OXIDOREDUCTASE;
PEROXIREDOXIN;
PROTEIN AHPF;
REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE;
THIOREDOXIN REDUCTASE;
UNCLASSIFIED DRUG;
ARTICLE;
DISULFIDE BOND;
ELECTRON TRANSPORT;
ENZYME ACTIVE SITE;
ENZYME ACTIVITY;
ENZYME ANALYSIS;
GENE CONSTRUCT;
GENE DISRUPTION;
GENETIC ENGINEERING;
NONHUMAN;
OXIDATION REDUCTION REACTION;
PRIORITY JOURNAL;
PROTEIN DOMAIN;
PROTEIN EXPRESSION;
PROTEIN FAMILY;
PROTEIN PURIFICATION;
CATALYSIS;
DIMERIZATION;
DITHIONITROBENZOIC ACID;
ELECTRON TRANSPORT;
ENZYME ACTIVATION;
FLAVIN-ADENINE DINUCLEOTIDE;
FLAVINS;
MUTAGENESIS, SITE-DIRECTED;
NAD;
OXIDATION-REDUCTION;
PEPTIDE FRAGMENTS;
PEROXIDASES;
PLASMIDS;
PROTEIN STRUCTURE, TERTIARY;
SALMONELLA TYPHIMURIUM;
SPECTROMETRY, FLUORESCENCE;
SPECTROPHOTOMETRY;
BACTERIA (MICROORGANISMS);
SALMONELLA TYPHIMURIUM;
TYPHIMURIUM;
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EID: 0035799368
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi002766h Document Type: Article |
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Times cited : (24)
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References (27)
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