Functional diversity of prokaryotic HdrA(BC) modules: Role in flavin-based electron bifurcation processes and beyond

In methanogenic archaea, the archetypical complex of heterodisulfide reductase (HdrABC) and hydrogenase (MvhAGD) couples the endergonic reduction of CO2 by H2 to the exergonic reduction of the CoB-S-S-CoM heterodisulfide by H2 via flavin-based electron bifurcation. Presently known enzymes containing...

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Published in:Biochimica et biophysica acta. Bioenergetics 2021-04, Vol.1862 (4), p.148379-148379, Article 148379
Main Authors: Appel, Lena, Willistein, Max, Dahl, Christiane, Ermler, Ulrich, Boll, Matthias
Format: Article
Language:English
Subjects:
Anaerobic metabolism
Archaea
architecture
aromatic compounds
carbon dioxide
crystal structure
degradation
electron transfer
energy
Energy coupling
Energy metabolism
enzymes
fermentation
Flavin-based electron bifurcation
functional diversity
Heterodisulfide reductase
methane production
methanogens
oxidation
Oxidoreductases
sulfates
sulfur compounds
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Summary:In methanogenic archaea, the archetypical complex of heterodisulfide reductase (HdrABC) and hydrogenase (MvhAGD) couples the endergonic reduction of CO2 by H2 to the exergonic reduction of the CoB-S-S-CoM heterodisulfide by H2 via flavin-based electron bifurcation. Presently known enzymes containing HdrA(BC)-like components play key roles in methanogenesis, acetogenesis, respiratory sulfate reduction, lithotrophic reduced sulfur compound oxidation, aromatic compound degradation, fermentations, and probably many further processes. This functional diversity is achieved by a modular architecture of HdrA(BC) enzymes, where a big variety of electron input/output modules may be connected either directly or via adaptor modules to the HdrA(BC) components. Many, but not all HdrA(BC) complexes are proposed to catalyse a flavin-based electron bifurcation/confurcation. Despite the availability of HdrA(BC) crystal structures, fundamental questions of electron transfer and energy coupling processes remain. Here, we address the common properties and functional diversity of HdrA(BC) core modules integrated into electron-transfer machineries of outstanding complexity. [Display omitted] •HdrA(BC) protein modules have originally been identified as heterodisulfide reductases in methanogenic archaea•Today, HdrA(BC) modules are known to play key roles in many types of archeal and bacterial metabolism•HdrA modules are highly complex electron transfer machineries in nature containing flavin and FeS cofactors•Many HdrA(BC) containing electron transfer machineries are involved in flavin-based electron bifurcation processes
ISSN:0005-2728
1879-2650
DOI:10.1016/j.bbabio.2021.148379