title: The Biological Methane-Forming Reaction: Mechanism Confirmed Through Spectroscopic Characterization of a Key Intermediate.
abstract: Find your path: Methyl-coenzyme M reductase (MCR, turquoise) reversibly catalyzes the reduction of methyl-coenzyme M (methyl-S-CoM) with coenzyme B (CoB-SH) to form methane and the heterodisulfide. Recently, spectroscopic methods were used to detect trapped intermediates in a stopped-flow system, and CoM-S-NiIIwas identified after half a turnover of the MCR reaction (F430=nickel porphinoid). This finding supports a methyl-radical catalytic mechanism.
authors: Max Planck Institute für terrestrische Mikrobiologie, Karl-von-Frisch Straße 10, 35043, Marburg, Germany. shima@mpi-marburg.mpg.de.|CREST, Japan Science and Technology Agency (JST), Saitama, Japan. shima@mpi-marburg.mpg.de.
authors: Seigo
authors: S
authors: Shima
mesh_terms: D004578:Electron Spin Resonance Spectroscopy; D015080:Mesna / Q000031:analogs & derivatives* / Q000378:metabolism; D008697:Methane / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D015394:Molecular Structure; D010769:Phosphothreonine / Q000031:analogs & derivatives* / Q000378:metabolism
chemical_list: C049349:7-mercaptoheptanoylthreonine phosphate; D010769:Phosphothreonine; C023349:methyl coenzyme M; D015080:Mesna; D008697:Methane
keywords: enzyme catalysis; metalloenzymes; methanogensis; methyl-coenzyme M reductase; protein structures