Katalog Plus
Bibliothek der Frankfurt UAS
Bald neuer Katalog: sichern Sie sich schon vorab Ihre persönlichen Merklisten im Nutzerkonto: Anleitung.
Dieses Ergebnis aus BASE kann Gästen nicht angezeigt werden.  Login für vollen Zugriff.

Evolution and diversity of oxidoreductases involved in redox balance and energy conservation

Title: Evolution and diversity of oxidoreductases involved in redox balance and energy conservation
Authors: Garcia, Pierre Simon; de Anda, Valerie; Baker, Brett; Gribaldo, Simonetta; Borrel, Guillaume
Contributors: Biologie Évolutive de la Cellule Microbienne - Evolutionary Biology of the Microbial Cell; Université Paris Cité (UPCité)-Microbiologie Intégrative et Moléculaire (UMR6047); Institut Pasteur Paris (IP)-Centre National de la Recherche Scientifique (CNRS)-Institut Pasteur Paris (IP)-Centre National de la Recherche Scientifique (CNRS); Laboratoire de chimie bactérienne (LCB); Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS); University of Texas at Austin Austin; Universität Wien = University of Vienna; This work was supported by the French National Agency for Research (grant nos. Methevol ANR-19-CE02-0005-01 and ANR LBX-62 IBEID GRANT INTRA LABEX) and by the Moore-Simons Project on the Origin of the Eukaryotic Cell, Simons Foundation grant no. 73592LPI (https://doi.org/10.46714/735925LPI) (to B.J.B.) and a Simons Foundation investigator award LI-SIAME-00002001 (to B.J.B.).; ANR-19-CE02-0005,METHEVOL,Caractérisation de nouveaux acteurs et des transitions évolutives dans le métabolisme du méthane, un métabolisme clef dans l'évolution du domaine Archaea(2019); ANR-10-LABX-0062,IBEID,Integrative Biology of Emerging Infectious Diseases(2010)
Source: ISSN: 2397-334X ; Nature Ecology & Evolution ; https://pasteur.hal.science/pasteur-05549434 ; Nature Ecology & Evolution, 2026, 10 (3), pp.550-565. ⟨10.1038/s41559-025-02969-0⟩.
Publisher Information: CCSD; Nature
Publication Year: 2026
Subject Terms: [SDV]Life Sciences [q-bio]
Description: International audience ; The regulation of redox balance and energy conservation is fundamental to life and relies on a large evolutionary network of oxidoreductases forming homologous protein complexes, collectively termed HORBEC (homologous oxidoreductase complexes involved in redox balance and energy conservation). These include hydrogenases, respiratory complex I and electron-bifurcating complexes, central to respiration, fermentation and methanogenesis. Despite their crucial role, a comprehensive investigation of the diversity and evolutionary history of HORBEC has been lacking. Here we exhaustively identified and analysed over 50 protein families representing all HORBEC components across thousands of bacterial and archaeal genomes. We propose a unified nomenclature and classification encompassing 31 complexes and provide an annotation tool. We highlight the extensive diversity of HORBEC, especially in Archaea. We provide information on overlooked systems and identify a new one probably acting as a cation transport platform. We show that HORBEC originated via extensive tinkering of ancestral modules, driven by strong evolutionary constraints. Finally, we infer the presence of respiratory complex I in the last universal common ancestor, opening questions on its potential role in early energy metabolisms. This work provides an evolutionary framework for HORBEC, representing a fundamental resource to predict and study redox metabolisms of ecological and biotechnological significance.
Document Type: article in journal/newspaper
Language: English
Relation: https://doi.org/10.6084/m9.figshare.30090436; info:eu-repo/semantics/altIdentifier/pmid/41634230; PUBMED: 41634230
DOI: 10.1038/s41559-025-02969-0
Availability: https://pasteur.hal.science/pasteur-05549434; https://pasteur.hal.science/pasteur-05549434v1/document; https://pasteur.hal.science/pasteur-05549434v1/file/Garcia_et_al_main_text_fig.pdf; https://doi.org/10.1038/s41559-025-02969-0
Rights: https://creativecommons.org/licenses/by/4.0/ ; info:eu-repo/semantics/OpenAccess
Accession Number: edsbas.FA8649B9
Database: BASE