| Literature DB >> 21438550 |
Peder E Cedervall1, Mishtu Dey, Xianghui Li, Ritimukta Sarangi, Britt Hedman, Stephen W Ragsdale, Carrie M Wilmot.
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 F(430). 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.Entities:
Mesh:
Substances:
Year: 2011 PMID: 21438550 PMCID: PMC3086036 DOI: 10.1021/ja110492p
Source DB: PubMed Journal: J Am Chem Soc ISSN: 0002-7863 Impact factor: 15.419