title: 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.
authors: Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota 55455, United States.
authors: Peder E
authors: PE
authors: Cedervall
authors: Mishtu
authors: M
authors: Dey
authors: Xianghui
authors: X
authors: Li
authors: Ritimukta
authors: R
authors: Sarangi
authors: Britt
authors: B
authors: Hedman
authors: Stephen W
authors: SW
authors: Ragsdale
authors: Carrie M
authors: CM
authors: Wilmot
mesh_terms: D001665:Binding Sites; D018360:Crystallography, X-Ray; D017013:Methanobacteriaceae / Q000201:enzymology*; D008958:Models, Molecular; D009532:Nickel / Q000378:metabolism; D010088:Oxidoreductases / Q000737:chemistry* / Q000378:metabolism
chemical_list: D009532:Nickel; D010088:Oxidoreductases; C021572:methyl coenzyme M reductase