Energy-converting hydrogenases: the link between H2 metabolism and energy conservation.
Cell Mol Life Sci
; 77(8): 1461-1481, 2020 Apr.
Article
em En
| MEDLINE
| ID: mdl-31630229
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 ([Formula see text]). The [Formula see text] 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.
Palavras-chave
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Bactérias
/
Archaea
/
Hidrogênio
/
Hidrogenase
Idioma:
En
Ano de publicação:
2020
Tipo de documento:
Article