Indole hydroxylation by bacterial cytochrome P450 BM-3 and modulation of activity by cumene hydroperoxide

Bioscience, Biotechnology and Biochemistry

Volumn 69, Issue 2, 2005, Pages 293-300

  Li, Qing Shan ^a   Ogawa, Jun ^a   Schmid, Rolf D ^b   Shimizu, Sakayu ^a  

^a KYOTO UNIVERSITY   (Japan)

^b UNIVERSITY OF STUTTGART   (Germany)

Author keywords

Cooperativity; Cumene hydroperoxide; Cytochrome P450; P450 BM 3; Peroxide shunt pathway

Indexed keywords

CATALYSIS; CONCENTRATION (PROCESS); ENZYME KINETICS; HYDROGEN PEROXIDE; HYDROXYLATION; REACTION KINETICS;

ALKALINE CONDITIONS; HETEROTROPIC COOPERATIVITY; HILL COEFFICIENT; HOMOTROPIC COOPERATIVITY;

PIGMENTS;

BENZENE DERIVATIVE; CUMENE HYDROPEROXIDE; CYTOCHROME P450; INDOLE DERIVATIVE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

ALLOSTERISM; ARTICLE; BACILLUS MEGATERIUM; BINDING SITE; CHEMISTRY; ENZYMOLOGY; GENETICS; HYDROXYLATION; METABOLISM; PH; POINT MUTATION;

ALLOSTERIC REGULATION; BACILLUS MEGATERIUM; BENZENE DERIVATIVES; BINDING SITES; CYTOCHROME P-450 ENZYME SYSTEM; HYDROGEN-ION CONCENTRATION; HYDROXYLATION; INDOLES; NADP; POINT MUTATION;

BACILLUS MEGATERIUM; BACTERIA (MICROORGANISMS);

EID: 15744398069     PISSN: 09168451     EISSN: None     Source Type: Journal    
DOI: 10.1271/bbb.69.293     Document Type: Article

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