Abstract
The reversible interconversion of molecular hydrogen and protons is one of the most ancient microbial metabolic reactions and catalyzed by hydrogenases. A widespread yet largely enigmatic group comprises multisubunit [NiFe] hydrogenases, that directly couple H2 metabolism to the electrochemical ion gradient across the membranes of bacteria and of archaea. These complexes are collectively referred to as energy-converting hydrogenases (Ech), as they reversibly transform redox energy into physicochemical energy. Redox energy is typically provided by a low potential electron donor such as reduced ferredoxin to fuel H2 evolution and the establishment of a transmembrane electrochemical ion gradient (\(\Delta \tilde{\mu }_{\text{ion}}\)). The \(\Delta \tilde{\mu }_{\text{ion}}\) is then utilized by an ATP synthase for energy conservation by generating ATP. This review describes the modular structure/function of Ech complexes, focuses on insights into the energy-converting mechanisms, describes the evolutionary context and delves into the implications of relying on an Ech complex as respiratory enzyme for microbial metabolism.
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Abbreviations
- \(\Delta G_{0}{}^{\prime }\) :
-
Gibbs free energy change under standard conditions
- \(\Delta \tilde{\mu }_{\text{ion}}\) :
-
Transmembrane electrochemical ion gradient
- Δψ :
-
Membrane potential
- Coo:
-
CO-oxidizing hydrogenase
- \(E_{0}{}^{{\prime }}\) :
-
Redox potential under standard conditions but pH 7.0
- Ech:
-
Energy-converting hydrogenase
- Ech1:
-
CO-oxidizing energy-converting hydrogenase 1 from T. kivui
- F420 :
-
Coenzyme F420
- FBEB:
-
Flavin-based electron bifurcation
- Fd:
-
Ferredoxin
- Fhl:
-
Formate hydrogen lyase
- Fpo:
-
F420H2 dehydrogenase
- MAF:
-
Mixed acid fermentation
- Mrp:
-
Multiple resistance and pH
- Nuo/Nqo:
-
NADH:ubiquinone/quinone oxidoreductase
- Pfl:
-
Pyruvate-formate lyase
- pH2 :
-
Hydrogen partial pressure
- Rnf:
-
Ferredoxin:NAD oxidoreductase
- SLP:
-
Substrate-level-phosphorylation
- WLP:
-
Wood–Ljungdahl pathway
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Work from the authors’ laboratory was supported by the Deutsche Forschungsgemeinschaft. MCS is a recipient of a fellowship by the Claussen-Simon-Stiftung (DE).
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Schoelmerich, M.C., Müller, V. Energy-converting hydrogenases: the link between H2 metabolism and energy conservation. Cell. Mol. Life Sci. 77, 1461–1481 (2020). https://doi.org/10.1007/s00018-019-03329-5
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DOI: https://doi.org/10.1007/s00018-019-03329-5