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A conspicuous nickel protein in microbial mats that oxidize methane anaerobically
The abundance of the nickel protein (7% of extracted proteins) in the mat suggests an important role in AOM, and similarities to methyl-coenzyme M reductase from methanogenic archaea are revealed.
Denitrifying bacteria anaerobically oxidize methane in the absence of Archaea.
The results show that bacteria can couple the anaerobic oxidation of methane to denitrification without the involvement of Archaea.
Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation.
Together with a second structurally characterized enzyme state (MCRsilent) containing the heterodisulfide of coenzymes M and B, a reaction mechanism is proposed that uses a radical intermediate and a nickel organic compound.
Hydrogenases from methanogenic archaea, nickel, a novel cofactor, and H2 storage.
- R. Thauer, Anne-Kristin Kaster, Meike Goenrich, M. Schick, T. Hiromoto, S. Shima
- Chemistry, BiologyAnnual Review of Biochemistry
- 9 June 2010
The formation of methane from 4 H( 2) and CO(2) catalyzed by methanogenic archaea is being discussed as an efficient means to store H(2), and putative genes for the synthesis of the FeGP cofactor have been identified.
Methane as Fuel for Anaerobic Microorganisms
There is evidence that anaerobic methane oxidation with sulfate proceeds at least in part via reversed methanogenesis involving the nickel enzyme methyl‐coenzyme M reductase for methane activation, which under standard conditions is an endergonic reaction, and thus inherently slow.
Hydrogenobacter acidophilus sp. nov., a Thermoacidophilic, Aerobic, Hydrogen-Oxidizing Bacterium Requiring Elemental Sulfur for Growth
A thermoacidophilic, obligately chemolithoautotrophic, aerobic, hydrogen-oxidizing bacterium, strain 3H-1T(T = type strain), was isolated from a solfataric field in Tsumagoi, Japan. This strain is a…
Mode of action uncovered for the specific reduction of methane emissions from ruminants by the small molecule 3-nitrooxypropanol
- E. Duin, T. Wagner, M. Kindermann
- Medicine, ChemistryProceedings of the National Academy of Sciences
- 2 May 2016
This study elucidates the development and the unique mode of action of the highly specific inhibitor 3-nitrooxypropanol (3-NOP), which is targeting the nickel enzyme methyl-coenzyme M reductase in rumen archaea that catalyzes the methane-forming reaction.
Coenzyme binding in F420-dependent secondary alcohol dehydrogenase, a member of the bacterial luciferase family.
Methanogenic heterodisulfide reductase (HdrABC-MvhAGD) uses two noncubane [4Fe-4S] clusters for reduction
The structure shows how two noncubane [4Fe-4S] clusters perform disulfide cleavage and gives insight into the mechanism of FBEB, the enzyme that reduces the disulfides and couples this to the reduction of ferredoxin in an energy-conserving process known as flavin-based electron bifurcation.
On the mechanism of biological methane formation: structural evidence for conformational changes in methyl-coenzyme M reductase upon substrate binding.
The binding of coen enzyme M induced specific conformational changes that postulate a molecular mechanism by which the enzyme ensures that methylcoenzyme M enters the substrate channel prior to coenzyme B as required by the active-site geometry.