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Volumn 35, Issue 47, 1996, Pages 15029-15037
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Functional interactions in cytochrome P450BM3. Fatty acid substrate binding alters electron-transfer properties of the flavoprotein domain
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Author keywords
[No Author keywords available]
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Indexed keywords
2,6 DICHLOROPHENOLINDOPHENOL;
CARBON MONOXIDE;
CYTOCHROME C;
CYTOCHROME P450;
CYTOCHROME P450 REDUCTASE;
FATTY ACID;
FERRICYANIDE;
FLAVINE ADENINE NUCLEOTIDE;
FLAVINE MONONUCLEOTIDE;
FLAVOPROTEIN;
HEME;
HYBRID PROTEIN;
LAURIC ACID;
OXYGEN;
OXYGENASE;
REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;
ARTICLE;
BINDING AFFINITY;
CATALYSIS;
CONFORMATIONAL TRANSITION;
CONTROLLED STUDY;
ELECTRON TRANSPORT;
ENZYME ACTIVITY;
ENZYME INHIBITION;
ESCHERICHIA COLI;
FLUORESCENCE;
HYDROXYLATION;
NONHUMAN;
PRIORITY JOURNAL;
BACTERIAL PROTEINS;
CARBON MONOXIDE;
CATALYSIS;
CYTOCHROME C GROUP;
CYTOCHROME P-450 ENZYME SYSTEM;
ELECTRON TRANSPORT;
ESCHERICHIA COLI;
FATTY ACIDS;
FLAVOPROTEINS;
HEME;
HYDROXYLATION;
LAURIC ACIDS;
MIXED FUNCTION OXYGENASES;
NADP;
OXIDATION-REDUCTION;
PROTEIN BINDING;
SPECTROMETRY, FLUORESCENCE;
BACTERIA (MICROORGANISMS);
ESCHERICHIA COLI;
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EID: 0030446061
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi961667u Document Type: Article |
Times cited : (40)
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References (29)
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