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Effects of Alternative Redox Partners and Oxidizing Agents on CYP154C8 Catalytic Activity and Product Distribution

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Title
Effects of Alternative Redox Partners and Oxidizing Agents on CYP154C8 Catalytic Activity and Product Distribution
Other Titles
CYP154C8 효소 특성 연구
Authors
Dangi, Bikash
Oh, Tae-Jin
Park, Hyun
Subject
Biochemistry & Molecular Biology; Pharmacology & Pharmacy
Keywords
CYP154C8; (diacetoxyiodo)benzene; cytochromes; electron transport; hydrogen; peroxide; hydroxylation; steroids
Issue Date
2018-11-02
Citation
Bikash Dangi, 오태진, Park, Hyun. 2018. "Effects of Alternative Redox Partners and Oxidizing Agents on CYP154C8 Catalytic Activity and Product Distribution". CHEMBIOCHEM, 19(21): 2273-2282.
Abstract
CYP154C8 catalyzes the hydroxylation of diverse steroids, as has previously been demonstrated, by using an NADH-dependent system including putidaredoxin and putidaredoxin reductase as redox partner proteins carrying electrons from NADH. In other reactions, CYP154C8 reconstituted with spinach ferredoxin and NADPH-dependent ferredoxin reductase displayed catalytic activity different from that of the NADH-dependent system. The NADPH-dependent system showed multistep oxidation of progesterone and other substrates including androstenedione, testosterone, and nandrolone. (Diacetoxyiodo)benzene was employed to generate compound I (FeO3+), actively supporting the redox reactions catalyzed by CYP154C8. In addition to 16a-hydroxylation, progesterone and 11-oxoprogesterone also underwent hydroxylation at the 6b-position in reactions supported by (diacetoxyiodo)benzene. CYP154C8 was active in the presence of high concentrations (>10 mm) of H2O2, with optimum conversion surprisingly being achieved at &75 mm H2O2. More importantly, H2O2 tolerance by CYP154C8 was evident in the very low heme oxidation rate constant (K) even at high concentrations of H2O2. Our results demonstrate that alternative redox partners and oxidizing agents influence the catalytic efficiency and product distribution of a cytochrome P450 enzyme. More importantly, these choices affected the type and selectivity of reaction catalyzed by the P450 enzyme
URI
http://repository.kopri.re.kr/handle/201206/9529
DOI
http://dx.doi.org/10.1002/cbic.201800284
ISSN
1439-4227
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