• Publications
  • Influence
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. Expand
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. Expand
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. Expand
Hydrogenases from methanogenic archaea, nickel, a novel cofactor, and H2 storage.
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. Expand
Methane as Fuel for Anaerobic Microorganisms
  • R. Thauer, S. Shima
  • Chemistry, Medicine
  • Annals of the New York Academy of Sciences
  • 1 March 2008
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. Expand
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 aExpand
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. Expand
Structure of coenzyme F420H2 oxidase (FprA), a di‐iron flavoprotein from methanogenic Archaea catalyzing the reduction of O2 to H2O
It is proposed that the redox‐dependent conformational change of the switch loop ensures alternate complete four‐electron O2 reduction and redox center re‐reduction in the inactive oxidized state. Expand
Coenzyme binding in F420-dependent secondary alcohol dehydrogenase, a member of the bacterial luciferase family.
The crystal structure of Adf from Methanoculleus thermophilicus at 1.8 A resolution in complex with a F(420)-acetone adduct is reported and isopropanol can be reliably modeled and a hydrogen transfer mechanism postulated. Expand
Comparison of three methyl-coenzyme M reductases from phylogenetically distant organisms: unusual amino acid modification, conservation and adaptation.
Analysis of the environment of the unusual amino acid residues near the active site of the methyl-coenzyme M reductase indicates that some of the modifications may be required for the enzyme to be catalytically effective. Expand