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Volumn 40, Issue 45, 2001, Pages 13439-13447
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Role of the conserved phenylalanine 181 of NADPH-cytochrome P450 oxidoreductase in FMN binding and catalytic activity
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Author keywords
[No Author keywords available]
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Indexed keywords
CYTOCHROMES;
BINDING ENERGY;
ESCHERICHIA COLI;
MUTAGENESIS;
SUBSTITUTION REACTIONS;
ENZYMES;
CYTOCHROME B5 REDUCTASE;
CYTOCHROME P450;
FLAVINE ADENINE NUCLEOTIDE;
FLAVINE MONONUCLEOTIDE;
GLUTAMINE;
LEUCINE;
OXIDOREDUCTASE;
PHENYLALANINE;
REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;
REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE FERRIHEMOPROTEIN REDUCTASE;
TYROSINE;
AMINO ACID SUBSTITUTION;
ARTICLE;
CATALYSIS;
COMPLEX FORMATION;
ENZYME ACTIVITY;
ENZYME ANALYSIS;
ESCHERICHIA COLI;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN BINDING;
PROTEIN STABILITY;
SITE DIRECTED MUTAGENESIS;
AMINO ACID SUBSTITUTION;
CATALYSIS;
CONSERVED SEQUENCE;
CYTOCHROME C GROUP;
FERRICYANIDES;
FLAVIN MONONUCLEOTIDE;
HUMANS;
MAGNETIC RESONANCE SPECTROSCOPY;
MODELS, MOLECULAR;
MUTAGENESIS;
NADPH-FERRIHEMOPROTEIN REDUCTASE;
OXIDATION-REDUCTION;
PHENYLALANINE;
ESCHERICHIA COLI;
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EID: 0035856519
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi011147l Document Type: Article |
Times cited : (12)
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References (42)
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