Role of subunit interactions in P450 oligomers in the loss of homotropic cooperativity in the cytochrome P450 3A4 mutant L211F/D214E/F304W

Archives of Biochemistry and Biophysics

Volumn 460, Issue 1, 2007, Pages 129-140

  Fernando, Harshica ^a   Davydov, Dmitri R ^a   Chin, Christopher C ^a   Halpert, James R ^a  

^a University of Texas Medical Branch School of Medicine   (United States)

Author keywords

1 Pyrenebutanol; Allostery; Apoprotein; Bromocryptine; Cooperativity; Cytochrome P450 3A4; Oligomers; Spin equilibrium; Substrate binding

Indexed keywords

1 PYRENEBUTANOL; ALPHA NAPHTHOFLAVONE; APOPROTEIN; BUTANOL; CYTOCHROME P450; D214E PROTEIN; F304W PROTEIN; GENE PRODUCT; HEME; L211F PROTEIN; PROGESTERONE; TESTOSTERONE; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; COOPERATION; DRUG MECHANISM; FLUORESCENCE RESONANCE ENERGY TRANSFER; HYDROXYLATION; MUTANT; NONHUMAN; PRIORITY JOURNAL; PROTEIN INTERACTION; TITRIMETRY;

APOPROTEINS; BINDING SITES; BROMOCRIPTINE; CYTOCHROME P-450 ENZYME SYSTEM; FLUORESCENCE RESONANCE ENERGY TRANSFER; HEMEPROTEINS; HYDROXYLATION; KINETICS; MUTATION; OXIDATION-REDUCTION; PROGESTERONE; PROTEIN SUBUNITS; PYRENES; SUBSTRATE SPECIFICITY; TESTOSTERONE;

EID: 33947595805     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2006.12.025     Document Type: Article

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