Catalysis by methyl-coenzyme M reductase: a theoretical study for heterodisulfide product formation

No abstract is available for this paper.

• Publication year

  2003

• Venue

  JBIC Journal of Biological Inorganic Chemistry

• Publication date

  2003-05-01

• Fields of study

  Medicine, Chemistry

• Identifiers
  DOI 10.1007/s00775-003-0461-8PMID 12728361
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Rapid ligand exchange in the MCRred1 form of methyl-coenzyme M reductase.

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• The porphyrin handbook

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• A mechanism from quantum chemical studies for methane formation in methanogenesis.

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• X-ray absorption and resonance Raman studies of methyl-coenzyme M reductase indicating that ligand exchange and macrocycle reduction accompany reductive activation.

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• Cryoreduction of methyl-coenzyme M reductase: EPR characterization of forms, MCR(ox1) and MCR (red1).

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• The substrate reaction mechanism of class III anaerobic ribonucleotide reductase

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• On the mechanism of biological methane formation: structural evidence for conformational changes in methyl-coenzyme M reductase upon substrate binding.

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• Comparison of three methyl-coenzyme M reductases from phylogenetically distant organisms: unusual amino acid modification, conservation and adaptation.

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• Biochemistry of methanogenesis: a tribute to Marjory Stephenson. 1998 Marjory Stephenson Prize Lecture.

  1998cited by this paper
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  1998cited by this paper
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• Purified methyl-coenzyme-M reductase is activated when the enzyme-bound coenzyme F430 is reduced to the nickel(I) oxidation state by titanium(III) citrate.

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• Reactions and Enzymes Involved in Methanogenesis from CO2 and H2

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• Purification of a cytochrome b containing H2:heterodisulfide oxidoreductase complex from membranes of Methanosarcina barkeri.

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• Evidence that the heterodisulfide of coenzyme M and 7-mercaptoheptanoylthreonine phosphate is a product of the methylreductase reaction in Methanobacterium.

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• Mid‐ and Far‐Infrared Marker Bands of the Metal Coordination Sites of the Histidine Side Chains in the Protein Cu,Zn‐Superoxide Dismutase

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  2006cites this paper
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• Spectroscopic and Kinetic Studies of the Reaction of Bromopropanesulfonate with Methyl-coenzyme M Reductase*

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• References

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• 29 Bioinorganic chemistry

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