Is There a Ni-Methyl Intermediate in the Mechanism of Methyl-Coenzyme M Reductase?

被引：31

作者：

Chen, Shi-lu ^{[1
]}

Pelmenschikov, Vladimir ^{[2
]}

Blomberg, Margareta R. A. ^{[1
]}

Siegbahn, Per E. M. ^{[1
]}

机构：

[1] Stockholm Univ, Dept Phys, SE-10691 Stockholm, Sweden

[2] Vrije Univ Amsterdam, Sci Comp & Modelling NV, NL-1081 HV Amsterdam, Netherlands

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2009年 / 131卷 / 29期

关键词：

BIOLOGICAL METHANE FORMATION; CONTINUUM DIELECTRIC THEORY; NICKEL-ALKYL BOND; ACTIVE-SITE; ENZYME; REACTIVITY; ENERGIES;

D O I：

10.1021/ja904301f

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The formation of methyl-Ni(F-430) species in methyl-coenzyme M reductase (MCR) has been investigated using the B3LYP hybrid density functional method and an active-site model built on the basis of X-ray crystal structure. CH3-I, CH3-Br, CH3-Cl, and CH3-S-CH3 were chosen as the substrates, the last one regarded as a model of the native substrate (methyl-coenzyme M, CH3-SCoM). The calculations indicate that the formation of CH3-Ni(F-430) in MCR is dependent on the acidity of the substrate leaving group. A CH3-Ni(F-430) species has been observed with methyl halides as substrates, while the formation of CH3-Ni(F-430) from the native substrate is demonstrated to be inaccessible energetically. These results agree well with the current experiments.

引用

页码：9912 / +

页数：3

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