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

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.

SUBMITTER: Cedervall PE 

PROVIDER: S-EPMC3086036 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature