Structural analysis of a Ni-methyl species in methyl-coenzyme M reductase from methanothermobacter marburgensis

Peder E. Cedervall, Mishtu Dey, Xianghui Li, Ritimukta Sarangi, Britt Hedman, Stephen W. Ragsdale, Carrie M. Wilmot

Research output: Contribution to journalArticlepeer-review

34 Scopus citations

Abstract

We present the 1.2 Å 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 Å 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.

Original languageEnglish (US)
Pages (from-to)5626-5628
Number of pages3
JournalJournal of the American Chemical Society
Volume133
Issue number15
DOIs
StatePublished - Apr 20 2011

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