Structural Analysis of a Ni-Methyl Species in Methyl-Coenzyme M Reductase from Methanothermobacter marburgensis

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• 作者：Peder E. Cedervall ; Mishtu Dey ; Xianghui Li ; Ritimukta Sarangi ; Britt Hedman ; Stephen W. Ragsdale ; Carrie M. Wilmot
• 刊名：Journal of the American Chemical Society
• 出版年：2011
• 出版时间：April 20, 2011
• 年：2011
• 卷：133
• 期：15
• 页码：5626-5628
• 全文大小：721K
• 年卷期：v.133,no.15(April 20, 2011)
• ISSN：1520-5126

文摘

We present the 1.2 脜 resolution X-ray crystal structure of a Ni-methyl species that is a proposed catalytic intermediate in methyl-coenzyme M reductase (MCR), the enzyme that catalyzes the biological formation of methane. The methyl group is situated 2.1 脜 proximal of the Ni atom of the MCR coenzyme F₄₃₀. A rearrangement of the substrate channel has been posited to bring together substrate species, but Ni(III)-methyl formation alone does not lead to any observable structural changes in the channel.