Redox loops in anaerobic respiration - The role of the widespread NrfD protein family and associated dimeric redox module.

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  • Additional Information
    • Source:
      Publisher: Elsevier Country of Publication: Netherlands NLM ID: 101731706 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1879-2650 (Electronic) Linking ISSN: 00052728 NLM ISO Abbreviation: Biochim Biophys Acta Bioenerg Subsets: MEDLINE
    • Publication Information:
      Original Publication: Amsterdam : Elsevier
    • Subject Terms:
      Cell Respiration* ; Energy Metabolism*; Electron Transport Complex I/*chemistry ; Electron Transport Complex I/*metabolism; Anaerobiosis ; Evolution, Molecular ; Oxidation-Reduction ; Protein Conformation
    • Abstract:
      In prokaryotes, the proton or sodium motive force required for ATP synthesis is produced by respiratory complexes that present an ion-pumping mechanism or are involved in redox loops performed by membrane proteins that usually have substrate and quinone-binding sites on opposite sides of the membrane. Some respiratory complexes include a dimeric redox module composed of a quinone-interacting membrane protein of the NrfD family and an iron‑sulfur protein of the NrfC family. The QrcABCD complex of sulfate reducers, which includes the QrcCD module homologous to NrfCD, was recently shown to perform electrogenic quinone reduction providing the first conclusive evidence for energy conservation among this family. Similar redox modules are present in multiple respiratory complexes, which can be associated with electroneutral, energy-driven or electrogenic reactions. This work discusses the presence of the NrfCD/PsrBC dimeric redox module in different bioenergetics contexts and its role in prokaryotic energy conservation mechanisms.
      (Copyright © 2021 Elsevier B.V. All rights reserved.)
    • Contributed Indexing:
      Keywords: Bioenergetics; Energy conservation; Quinone oxidoreductase complexes
    • Accession Number:
      EC 7.1.1.2 (Electron Transport Complex I)
    • Publication Date:
      Date Created: 20210323 Date Completed: 20210924 Latest Revision: 20210924
    • Publication Date:
      20240829
    • Accession Number:
      10.1016/j.bbabio.2021.148416
    • Accession Number:
      33753023