The Ion-Translocating NrfD-Like Subunit of Energy-Transducing Membrane Complexes.

CISM family NrfD-like energy transduction ion translocation membrane protein quinine/quinol binding site

Journal

Frontiers in chemistry
ISSN: 2296-2646
Titre abrégé: Front Chem
Pays: Switzerland
ID NLM: 101627988

Informations de publication

Date de publication:
2021
Historique:
received: 03 02 2021
accepted: 19 03 2021
entrez: 30 4 2021
pubmed: 1 5 2021
medline: 1 5 2021
Statut: epublish

Résumé

Several energy-transducing microbial enzymes have their peripheral subunits connected to the membrane through an integral membrane protein, that interacts with quinones but does not have redox cofactors, the so-called NrfD-like subunit. The periplasmic nitrite reductase (NrfABCD) was the first complex recognized to have a membrane subunit with these characteristics and consequently provided the family's name: NrfD. Sequence analyses indicate that NrfD homologs are present in many diverse enzymes, such as polysulfide reductase (PsrABC), respiratory alternative complex III (ACIII), dimethyl sulfoxide (DMSO) reductase (DmsABC), tetrathionate reductase (TtrABC), sulfur reductase complex (SreABC), sulfite dehydrogenase (SoeABC), quinone reductase complex (QrcABCD), nine-heme cytochrome complex (NhcABCD), group-2 [NiFe] hydrogenase (Hyd-2), dissimilatory sulfite-reductase complex (DsrMKJOP), arsenate reductase (ArrC) and multiheme cytochrome

Identifiants

pubmed: 33928068
doi: 10.3389/fchem.2021.663706
pmc: PMC8076601
doi:

Types de publication

Journal Article

Langues

eng

Pagination

663706

Informations de copyright

Copyright © 2021 Calisto and Pereira.

Déclaration de conflit d'intérêts

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

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Auteurs

Filipa Calisto (F)

Instituto de Tecnologia Química e Biológica-António Xavier, Universidade Nova de Lisboa, Oeiras, Portugal.
BioISI-Biosystems & Integrative Sciences Institute, Faculdade de Ciências, Universdade de Lisboa, Lisboa, Portugal.

Manuela M Pereira (MM)

Instituto de Tecnologia Química e Biológica-António Xavier, Universidade Nova de Lisboa, Oeiras, Portugal.
BioISI-Biosystems & Integrative Sciences Institute, Faculdade de Ciências, Universdade de Lisboa, Lisboa, Portugal.

Classifications MeSH