Hydrocarbon Hydroxylation by Cytochrome P450 Enzymes

被引:907
作者
de Montellano, Paul R. Ortiz [1 ]
机构
[1] Univ Calif San Francisco, Dept Pharmaceut Chem, San Francisco, CA 94158 USA
基金
美国国家卫生研究院;
关键词
COMPOUND-I FORMATION; BOND-DISSOCIATION ENTHALPIES; CRYSTAL-STRUCTURE; RESONANCE RAMAN; VALPROIC ACID; SODIUM PERIODATE; FATTY-ACIDS; RAT-LIVER; WILD-TYPE; THERMOPHILIC CYTOCHROME-P450;
D O I
10.1021/cr9002193
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
A study was conducted to demonstrate hydrocarbon hydroxylation by cytochrome P450 enzymes. The cytochrome P450 enzymes were defined by the presence in the proteins heme prosthetic group coordinated on the proximal side by a thiolate ion. Investigations revealed that the principles of cytochrome P450 enzymes hydrocarbon hydroxylation applied to other hydroxylation reactions, including those that occurred on carbons adjacent to nitrogen, sulfur, or oxygen. The P450 enzyme was in the ferric state and had a thiolate proximal ligand and the distal ligand was a water molecule. Reduction in the ferrous enzyme was followed by binding of molecular oxygen to give the ferrous dioxy complex. This complex was observed and characterized by P450cam by diverse physical techniques.
引用
收藏
页码:932 / 948
页数:17
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