NiII(dioxo[16]aneN5)-induced methane formation from methyl coenzyme M
نویسندگان
چکیده
منابع مشابه
Identification of methyl coenzyme M reductase A (mcrA) genes associated with methane-oxidizing archaea.
Phylogenetic and stable-isotope analyses implicated two methanogen-like archaeal groups, ANME-1 and ANME-2, as key participants in the process of anaerobic methane oxidation. Although nothing is known about anaerobic methane oxidation at the molecular level, the evolutionary relationship between methane-oxidizing archaea (MOA) and methanogenic archaea raises the possibility that MOA have co-opt...
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 کاملPhylogenetic diversity of methyl-coenzyme M reductase (mcrA) gene and methanogenesis from trimethylamine in hypersaline environments.
Methanogens have been reported in complex microbial communities from hypersaline environments, but little is known about their phylogenetic diversity. In this work, methane concentrations in environmental gas samples were determined while methane production rates were measured in microcosm experiments with competitive and non-competitive substrates. In addition, the phylogenetic diversity of me...
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 کاملGeometric and Electronic Structures of the Ni(I) and Methyl-Ni(III) Intermediates of Methyl-Coenzyme M Reductase
Methyl-coenzyme M reductase (MCR) from methanogenic archaea catalyzes the terminal step in biological methane synthesis. Using coenzyme B (CoBSH) as the two-electron donor, MCR reduces methyl-coenzyme M (methyl-SCoM) to form methane and the heterodisulfide product, CoBS-SCoM. MCR contains an essential redox active nickel tetrapyrrolic cofactor called coenzyme F430 at its active site, which is a...
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ژورنال
عنوان ژورنال: Inorganic Chemistry
سال: 1988
ISSN: 0020-1669,1520-510X
DOI: 10.1021/ic00287a005