Energy-converting hydrogenases: the link between H2 metabolism and energy conservation
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Date
2020-04
Publication Type
Review Article
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no
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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 (Δμ~ion
). The Δμ~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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published
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Journal / series
Volume
77 (8)
Pages / Article No.
1461 - 1481
Publisher
Springer
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Subject
Energy-converting hydrogenase; Hydrogenases; Energy conservation; Respiratory mechanism; Bioenergetics
Organisational unit
09817 - Schoelmerich, Marie / Schoelmerich, Marie