The Reaction Mechanism of Methyl-Coenzyme M Reductase
نویسندگان
چکیده
منابع مشابه
The reaction mechanism of methyl-coenzyme M reductase: how an enzyme enforces strict binding order.
Methyl-coenzyme M reductase (MCR) is a nickel tetrahydrocorphinoid (coenzyme F430) containing enzyme involved in the biological synthesis and anaerobic oxidation of methane. MCR catalyzes the conversion of methyl-2-mercaptoethanesulfonate (methyl-SCoM) and N-7-mercaptoheptanoylthreonine phosphate (CoB7SH) to CH4 and the mixed disulfide CoBS-SCoM. In this study, the reaction of MCR from Methanot...
متن کاملElucidating the process of activation of methyl-coenzyme M reductase.
Methyl-coenzyme M reductase (MCR) catalyzes the reversible reduction of methyl-coenzyme M (CH3-S-CoM) and coenzyme B (HS-CoB) to methane and heterodisulfide CoM-S-S-CoB (HDS). MCR contains the hydroporphinoid nickel complex coenzyme F430 in its active site, and the Ni center has to be in its Ni(I) valence state for the enzyme to be active. Until now, no in vitro method that fully converted the ...
متن کاملGeometric and Electronic Structures of the NiI and Methyl−NiIII Intermediates of Methyl-Coenzyme M Reductase†
Methyl-coenzyme M reductase (MCR) catalyzes the terminal step in the formation of biological methane from methyl-coenzyme M (Me-SCoM) and coenzyme B (CoBSH). The active site in MCR contains a Ni-F(430) cofactor, which can exist in different oxidation states. The catalytic mechanism of methane formation has remained elusive despite intense spectroscopic and theoretical investigations. On the bas...
متن کاملThe biosynthesis of methylated amino acids in the active site region of methyl-coenzyme M reductase.
The global production of the greenhouse gas methane by methanogenic archaea reaches 1 billion tons per annum. The final reaction releasing methane is catalyzed by the enzyme methyl-coenzyme M reductase. The crystal structure of methyl-coenzyme M reductase from Methanobacterium thermoautotrophicum revealed the presence of five modified amino acids within the alpha-subunit and near the active sit...
متن کاملThe mechanism of action of cobamide coenzyme in the ribonucleotide reductase reaction.
When highly purified cobamide-dependent ribonucleotide reductase from Lacfobacillus leichmannii is incubated with synthetically prepared 5,6-dimethylbenzimidazolylcobamide 5’-deoxyadenosyl coenzyme containing tritium attached to carbon atom 5’ of the deoxyadenosyl moiety (DBCC-5’-3H), tritium is transferred from DBCC-5’-3H to Hz0 in a reaction requiring substrate, enzyme, and dithiol reductant....
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2015
ISSN: 0021-9258
DOI: 10.1074/jbc.m115.636761