» Articles » PMID: 7747931

Metabolism of Methanogens

Overview
Publisher Springer
Specialty Microbiology
Date 1994 Jan 1
PMID 7747931
Citations 25
Authors
Affiliations
Soon will be listed here.
Abstract

Methanogenic archaea convert a few simple compounds such as H2 + CO2, formate, methanol, methylamines, and acetate to methane. Methanogenesis from all these substrates requires a number of unique coenzymes, some of which are exclusively found in methanogens. H2-dependent CO2 reduction proceeds via carrier-bound C1 intermediates which become stepwise reduced to methane. Methane formation from methanol and methylamines involves the disproportionation of the methyl groups. Part of the methyl groups are oxidized to CO2, and the reducing equivalents thereby gained are subsequently used to reduce other methyl groups to methane. This process involves the same C1 intermediates that are formed during methanogenesis from CO2. Conversion of acetate to methane and carbon dioxide is preceded by its activation to acetyl-CoA. Cleavage of the latter compound yields a coenzyme-bound methyl moiety and an enzyme-bound carbonyl group. The reducing equivalents gained by oxidation of the carbonyl group to carbon dioxide are subsequently used to reduce the methyl moiety to methane. All these processes lead to the generation of transmembrane ion gradients which fuel ATP synthesis via one or two types of ATP synthases. The synthesis of cellular building blocks starts with the central anabolic intermediate acetyl-CoA which, in autotrophic methanogens, is synthesized from two molecules of CO2 in a linear pathway.

Citing Articles

The human gut microbiome in health and disease: time for a new chapter?.

Lee J, Bays D, Savage H, Baumler A Infect Immun. 2024; 92(11):e0030224.

PMID: 39347570 PMC: 11556149. DOI: 10.1128/iai.00302-24.


The effect of , , and on ruminal methanogenesis and metagenomic functional profiles .

Yergaliyev T, Kunzel S, Hanauska A, Rees A, Wild K, Petursdottir A Microbiol Spectr. 2024; 12(11):e0394223.

PMID: 39347544 PMC: 11542596. DOI: 10.1128/spectrum.03942-23.


Leafcutter ants enhance microbial drought resilience in tropical forest soil.

Shulman H, Aronson E, Dierick D, Pinto-Tomas A, Botthoff J, Artavia-Leon A Environ Microbiol Rep. 2024; 16(3):e13251.

PMID: 38778789 PMC: 11112399. DOI: 10.1111/1758-2229.13251.


Effect of Antimicrobial Use in Conventional Versus Natural Cattle Feedlots on the Microbiome and Resistome.

Lee C, Zaheer R, Munns K, Holman D, Van Domselaar G, Zovoilis A Microorganisms. 2023; 11(12).

PMID: 38138126 PMC: 10745953. DOI: 10.3390/microorganisms11122982.


Contrasting Fecal Methanogenic and Bacterial Profiles of Organic Dairy Cows Located in Northwest Washington Receiving Either a Mixed Diet of Pasture and TMR or Solely TMR.

Slanzon G, Sischo W, McConnel C Animals (Basel). 2022; 12(20).

PMID: 36290156 PMC: 9597778. DOI: 10.3390/ani12202771.


References
1.
Bobik T, Olson K, Noll K, WOLFE R . Evidence that the heterodisulfide of coenzyme M and 7-mercaptoheptanoylthreonine phosphate is a product of the methylreductase reaction in Methanobacterium. Biochem Biophys Res Commun. 1987; 149(2):455-60. DOI: 10.1016/0006-291x(87)90389-5. View

2.
Mayer F, Rohde M, Salzmann M, Jussofie A, Gottschalk G . The methanoreductosome: a high-molecular-weight enzyme complex in the methanogenic bacterium strain Gö1 that contains components of the methylreductase system. J Bacteriol. 1988; 170(4):1438-44. PMC: 210986. DOI: 10.1128/jb.170.4.1438-1444.1988. View

3.
Inatomi K . Characterization and purification of the membrane-bound ATPase of the archaebacterium Methanosarcina barkeri. J Bacteriol. 1986; 167(3):837-41. PMC: 215949. DOI: 10.1128/jb.167.3.837-841.1986. View

4.
Gogarten J, Rausch T, Bernasconi P, Kibak H, Taiz L . Molecular evolution of H+-ATPases. I. Methanococcus and Sulfolobus are monophyletic with respect to eukaryotes and Eubacteria. Z Naturforsch C J Biosci. 1989; 44(7-8):641-50. DOI: 10.1515/znc-1989-7-816. View

5.
Denda K, Konishi J, Oshima T, Date T, Yoshida M . Molecular cloning of the beta-subunit of a possible non-F0F1 type ATP synthase from the acidothermophilic archaebacterium, Sulfolobus acidocaldarius. J Biol Chem. 1988; 263(33):17251-4. View