Substrate binding and C-H bond activation in the soluble methane monooxygenase hydroxylase

被引：35

作者：

Whittington, DA ^{[1
]}

Valentine, AM ^{[1
]}

Lippard, SJ ^{[1
]}

机构：

[1] MIT, Dept Chem, Cambridge, MA 02139 USA

来源：

JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY | 1998年 / 3卷 / 03期

基金：

美国国家卫生研究院;

关键词：

oxygen activation; carboxylate-bridged diiron center; enzyme mechanism;

D O I：

10.1007/s007750050237

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The selective oxidation of CH4 to CH3OH is a conceptually simple, yet functionally difficult, chemical transformation. In nature, this reaction is performed by methane monooxygenases, the soluble class of which employ carboxylate-bridged dinuclear iron centers to activate dioxygen. The process by which small molecules access the active site of the sMMO hydroxylase, the structures of intermediates in the catalytic reaction cycle, and mechanistic details about the attack on the C-H bond are subjects of intense investigation. In this commentary, we present our current views on exogenous ligand binding and dioxygen activation at the active site and the mechanism of alkane hydroxylation.

引用

页码：307 / 313

页数：7