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The key nickel enzyme of methanogenesis catalyses the anaerobic oxidation of methane
TLDR
Purified MCR from Methanothermobacter marburgensis converts methane into methyl-coenzyme M under equilibrium conditions with apparent Vmax and Km values consistent with the observed in vivo kinetics of the anaerobic oxidation of methane with sulphate, which supports the hypothesis of ‘reverse methanogenesis’.
Hydrogenases from methanogenic archaea, nickel, a novel cofactor, and H2 storage.
TLDR
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.
An Ancient Pathway Combining Carbon Dioxide Fixation with the Generation and Utilization of a Sodium Ion Gradient for ATP Synthesis
TLDR
The genome sequence of A. woodii solves the enigma and uncovers Rnf as the only ion-motive enzyme coupled to the pathway and unravels a metabolism designed to produce reduced ferredoxin and overcome energetic barriers by virtue of electron-bifurcating, soluble enzymes.
A Glutathione-dependent Formaldehyde-activating Enzyme (Gfa) from Paracoccus denitrificans Detected and Purified via Two-dimensional Proton Exchange NMR Spectroscopy* 210
TLDR
The discovery of an enzyme from Paracoccus denitrificans that accelerates this spontaneous condensation reaction for S-hydroxymethylglutathione formation and cleavage is described.
More Than 200 Genes Required for Methane Formation from H2 and CO2 and Energy Conservation Are Present in Methanothermobacter marburgensis and Methanothermobacter thermautotrophicus
TLDR
Within the 1,607 protein coding sequences in common, approximately 200 CDS required for the synthesis of the enzymes, coenzymes, and prosthetic groups involved in CO2 reduction to methane and in coupling this process with the phosphorylation of ADP are identified.
Methyl-coenzyme M reductase from methanogenic archaea: isotope effects on the formation and anaerobic oxidation of methane.
TLDR
These values are consistent with isotope effects reported for oxidative cleavage/reductive coupling occurring at transition metal centers during C-H activation but are also in the range expected for the radical substitution mechanism proposed by Siegbahn et al.
Temperature dependence of methyl-coenzyme M reductase activity and of the formation of the methyl-coenzyme M reductase red2 state induced by coenzyme B
TLDR
Findings indicate that in the presence of both coenzyme M and coen enzyme B only one of the two active sites of MCR can be in the red2 state (half-of-the-sites reactivity), and a two-stroke engine mechanism for MCR is proposed.
Probing the reactivity of Ni in the active site of methyl-coenzyme M reductase with substrate analogues
TLDR
Experiments with methyl-coenzyme M analogues showing how they affect the activity and the MCR-red1 signal of MCR from Methanothermobacter marburgensis concluded that the Ni-based EPR spectra of both inactive forms were not affected in the presence of high concentrations of these two potent inhibitors.
A nickel hydride complex in the active site of methyl-coenzyme m reductase: implications for the catalytic cycle.
TLDR
It is believed that the nickel hydride complex reported here could play a key role in helping to understand both the mechanism of "reverse" and "forward" methanogenesis.
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