期刊
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
卷 409, 期 1, 页码 72-79出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/S0003-9861(02)00445-9
关键词
cytochrome P450; hydroxylation mechanism; activated oxygen; iron-oxo; hydroperoxo-iron
资金
- NATIONAL CANCER INSTITUTE [R01CA016954, R37CA016954] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES [R37DK010339, R01DK010339] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM048722] Funding Source: NIH RePORTER
- NCI NIH HHS [CA-16954] Funding Source: Medline
- NIDDK NIH HHS [DK-10339] Funding Source: Medline
- NIGMS NIH HHS [GM-48722] Funding Source: Medline
Cytochrome P450 enzymes catalyze a number of oxidations in nature including the difficult hydroxylations of unactivated positions in an alkyl group. The consensus view of the hydroxylation reaction 10 years ago was that a high valent iron-oxo species abstracts a hydrogen atom from the alkyl group to give a radical that subsequently displaces the hydroxy group from iron in a homolytic substitution reaction (hydrogen abstraction-oxygen rebound). More recent mechanistic studies, as summarized in this review, indicated that the cytochrome P450-catalyzed hydroxylation reaction is complex, involving multiple mechanisms and multiple oxidants. In addition to the iron-oxo species, another electrophilic oxidant apparently exists, either the hydroperoxo-iron intermediate that precedes iron-oxo or iron-complexed hydrogen peroxide formed by protonation of the hydroperoxo-iron species on the proximal oxygen. The other electrophilic oxidant appears to react by insertion of OH+ into a C-H bond to give a protonated alcohol. Computational work has suggested that iron-oxo can react through multiple spin states, a low-spin ensemble that reacts by insertion of oxygen, and a high-spin ensemble that reacts by hydrogen atom abstraction to give a radical. (C) 2002 Elsevier Science (USA). All rights reserved.
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