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Structural Basis of Hydrogenotrophic Methanogenesis.
- Source :
- Annual Review of Microbiology; Sep2020, Vol. 74, p713-733, 25p
- Publication Year :
- 2020
-
Abstract
- Most methanogenic archaea use the rudimentary hydrogenotrophic pathway—from CO<subscript>2</subscript> and H<subscript>2</subscript> to methane—as the terminal step of microbial biomass degradation in anoxic habitats. The barely exergonic process that just conserves sufficient energy for a modest lifestyle involves chemically challenging reactions catalyzed by complex enzyme machineries with unique metal-containing cofactors. The basic strategy of the methanogenic energy metabolism is to covalently bind C<subscript>1</subscript> species to the C<subscript>1</subscript> carriers methanofuran, tetrahydromethanopterin, and coenzyme M at different oxidation states. The four reduction reactions from CO<subscript>2</subscript> to methane involve one molybdopterin-based two-electron reduction, two coenzyme F<subscript>420</subscript>–based hydride transfers, and one coenzyme F<subscript>430</subscript>–based radical process. For energy conservation, one ion-gradient-forming methyl transfer reaction is sufficient, albeit supported by a sophisticated energy-coupling process termed flavin-based electron bifurcation for driving the endergonic CO<subscript>2</subscript> reduction and fixation. Here, we review the knowledge about the structure-based catalytic mechanism of each enzyme of hydrogenotrophic methanogenesis. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00664227
- Volume :
- 74
- Database :
- Complementary Index
- Journal :
- Annual Review of Microbiology
- Publication Type :
- Academic Journal
- Accession number :
- 145644539
- Full Text :
- https://doi.org/10.1146/annurev-micro-011720-122807