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Volumn 91, Issue 4, 2002, Pages 542-553
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Replacement of active-site cysteine-436 by serine converts cytochrome P450 2B4 into an NADPH oxidase with negligible monooxygenase activity
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Author keywords
Axial thiolate heme ligand; Cytochrome P450; Mutagenesis; Two electron oxidase
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Indexed keywords
1 PHENYLETHANOL;
4 FLUOROPHENOL;
4 NITROPHENOL;
AMINE;
CYSTEINE;
CYTOCHROME P450 2B;
CYTOCHROME P450 2E1;
ENZYME;
GUAIACOL;
HEME;
HEMOPROTEIN;
HYDROGEN PEROXIDE;
OXIDOREDUCTASE;
PHENOL DERIVATIVE;
PROTOPORPHYRIN;
PYRIDINE;
PYROGALLOL;
REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE;
SERINE;
UNCLASSIFIED DRUG;
UNSPECIFIC MONOOXYGENASE;
AMINO ACID ANALYSIS;
ARTICLE;
CATALYSIS;
CONCENTRATION (PARAMETERS);
ELECTRON;
ENZYME ACTIVITY;
ENZYME ANALYSIS;
HYDROXYLATION;
MUTAGENESIS;
PEROXIDATION;
PURIFICATION;
TIME;
WILD TYPE;
ARYL HYDROCARBON HYDROXYLASES;
BINDING SITES;
CLONING, MOLECULAR;
CYSTEINE;
HYDROGEN PEROXIDE;
MULTIENZYME COMPLEXES;
MUTAGENESIS, SITE-DIRECTED;
NADH, NADPH OXIDOREDUCTASES;
PEROXIDASES;
RECOMBINANT PROTEINS;
SEQUENCE DELETION;
SERINE;
SUBSTRATE SPECIFICITY;
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EID: 0037145063
PISSN: 01620134
EISSN: None
Source Type: Journal
DOI: 10.1016/S0162-0134(02)00438-5 Document Type: Article |
Times cited : (44)
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References (43)
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