Biochemistry of Methyl-Coenzyme M Reductase

Stephen W. Ragsdale, Simone Raugei, Bojana Ginovska, Thanyaporn Wongnate

Research output: Chapter in Book/Report/Conference proceedingChapter

1 Citation (Scopus)

Abstract

Methanogens are masters of CO2 reduction. They conserve energy by coupling H2 oxidation to the reduction of CO2 to CH4, the primary constituent of natural gas. They also generate methane by the reduction of acetic acid, methanol, methane thiol, and methylamines. Methanogens produce 109 tons of methane per year and are the major source of the earth's atmospheric methane. Reverse methanogenesis or anaerobic methane oxidation, which is catalyzed by methanotrophic archaea living in consortia among bacteria that can act as an electron acceptor, is responsible for annual oxidation of 108 tons of methane to CO2. This chapter briefly describes the overall process of methanogenesis and then describes the enzymatic mechanism of the nickel enzyme, methyl-CoM reductase (MCR), the key enzyme in methane synthesis and oxidation. MCR catalyzes the formation of methane and the heterodisulfide (CoBSSCoM) from methyl-coenzyme M (methyl-CoM) and coenzyme B (HSCoB). Uncovering the mechanistic and molecular details of MCR catalysis is critical since methane is an abundant and important fuel and is the second (to CO2) most prevalent greenhouse gas.

Original languageEnglish
Title of host publicationMolybdenum and Tungsten Enzymes: Biochemistry
PublisherRoyal Society of Chemistry
Pages149-169
Number of pages21
Volume2017-January
Edition10
DOIs
Publication statusPublished - 2017

Publication series

NameRSC Metallobiology
Number10
Volume2017-January
ISSN (Print)2045547X

Fingerprint

Biochemistry
Methane
Methanogens
Oxidation
Methylamines
Enzymes and Coenzymes
Natural Gas
methyl coenzyme M reductase
Archaea
Enzymes
Nickel
Catalysis
Sulfhydryl Compounds
Greenhouse gases
Acetic Acid
Methanol
Natural gas
Bacteria
Gases
Earth (planet)

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology (miscellaneous)

Cite this

Ragsdale, S. W., Raugei, S., Ginovska, B., & Wongnate, T. (2017). Biochemistry of Methyl-Coenzyme M Reductase. In Molybdenum and Tungsten Enzymes: Biochemistry (10 ed., Vol. 2017-January, pp. 149-169). (RSC Metallobiology; Vol. 2017-January, No. 10). Royal Society of Chemistry. https://doi.org/10.1039/9781788010580-00149

Biochemistry of Methyl-Coenzyme M Reductase. / Ragsdale, Stephen W.; Raugei, Simone; Ginovska, Bojana; Wongnate, Thanyaporn.

Molybdenum and Tungsten Enzymes: Biochemistry. Vol. 2017-January 10. ed. Royal Society of Chemistry, 2017. p. 149-169 (RSC Metallobiology; Vol. 2017-January, No. 10).

Research output: Chapter in Book/Report/Conference proceedingChapter

Ragsdale, SW, Raugei, S, Ginovska, B & Wongnate, T 2017, Biochemistry of Methyl-Coenzyme M Reductase. in Molybdenum and Tungsten Enzymes: Biochemistry. 10 edn, vol. 2017-January, RSC Metallobiology, no. 10, vol. 2017-January, Royal Society of Chemistry, pp. 149-169. https://doi.org/10.1039/9781788010580-00149
Ragsdale SW, Raugei S, Ginovska B, Wongnate T. Biochemistry of Methyl-Coenzyme M Reductase. In Molybdenum and Tungsten Enzymes: Biochemistry. 10 ed. Vol. 2017-January. Royal Society of Chemistry. 2017. p. 149-169. (RSC Metallobiology; 10). https://doi.org/10.1039/9781788010580-00149
Ragsdale, Stephen W. ; Raugei, Simone ; Ginovska, Bojana ; Wongnate, Thanyaporn. / Biochemistry of Methyl-Coenzyme M Reductase. Molybdenum and Tungsten Enzymes: Biochemistry. Vol. 2017-January 10. ed. Royal Society of Chemistry, 2017. pp. 149-169 (RSC Metallobiology; 10).
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