Periplasmic electron transfer network in Geobacter sulfurreducens revealed by biomolecular interaction studies.


Journal

Protein science : a publication of the Protein Society
ISSN: 1469-896X
Titre abrégé: Protein Sci
Pays: United States
ID NLM: 9211750

Informations de publication

Date de publication:
Jul 2024
Historique:
revised: 31 05 2024
received: 21 01 2024
accepted: 03 06 2024
medline: 27 6 2024
pubmed: 27 6 2024
entrez: 27 6 2024
Statut: ppublish

Résumé

Multiheme cytochromes located in different compartments are crucial for extracellular electron transfer in the bacterium Geobacter sulfurreducens to drive important environmental processes and biotechnological applications. Recent studies have unveiled that for particular sets of electron terminal acceptors, discrete respiratory pathways selectively recruit specific cytochromes from both the inner and outer membranes. However, such specificity was not observed for the abundant periplasmic cytochromes, namely the triheme cytochrome family PpcA-E. In this work, the distinctive NMR spectroscopic signatures of these proteins in different redox states were explored to monitor pairwise interactions and electron transfer reactions between each pair of cytochromes. The results showed that the five proteins interact transiently and can exchange electrons between each other revealing intra-promiscuity within the members of this family. This discovery is discussed in the light of the establishment of an effective electron transfer network by this pool of cytochromes. This network is advantageous to the bacteria as it enables the maintenance of the functional working potential redox range within the cells.

Identifiants

pubmed: 38935664
doi: 10.1002/pro.5082
doi:

Substances chimiques

Bacterial Proteins 0
Cytochromes 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

e5082

Subventions

Organisme : Fundação para a Ciência e Tecnologia (FCT)
ID : SFRH/BD/132969/2017
Organisme : Fundação para a Ciência e Tecnologia (FCT)
ID : PTDC/BIABQM/4967/2020
Organisme : Fundação para a Ciência e Tecnologia (FCT)
ID : EXPL/BIA-BQM/0770/2021
Organisme : Fundação para a Ciência e Tecnologia (FCT)
ID : UIDP/04378/2020
Organisme : Fundação para a Ciência e Tecnologia (FCT)
ID : UIDB/04378/2020
Organisme : Fundação para a Ciência e Tecnologia (FCT)
ID : LA/P/0140/2020
Organisme : Fundação para a Ciência e Tecnologia (FCT)
ID : ROTEIRO/0031/2013
Organisme : Fundação para a Ciência e Tecnologia (FCT)
ID : PINFRA/22161/2016
Organisme : Eurpean Regional Development Fund
Organisme : PIDDAC

Informations de copyright

© 2024 The Protein Society.

Références

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Auteurs

Marisa R Ferreira (MR)

Associate Laboratory i4HB - Institute for Health and Bioeconomy, NOVA School of Science and Technology, Universidade NOVA de Lisboa, Caparica, Portugal.
UCIBIO - Applied Molecular Biosciences Unit, Department of Chemistry, NOVA School of Science and Technology, Universidade NOVA de Lisboa, Caparica, Portugal.

Leonor Morgado (L)

Associate Laboratory i4HB - Institute for Health and Bioeconomy, NOVA School of Science and Technology, Universidade NOVA de Lisboa, Caparica, Portugal.
UCIBIO - Applied Molecular Biosciences Unit, Department of Chemistry, NOVA School of Science and Technology, Universidade NOVA de Lisboa, Caparica, Portugal.

Carlos A Salgueiro (CA)

Associate Laboratory i4HB - Institute for Health and Bioeconomy, NOVA School of Science and Technology, Universidade NOVA de Lisboa, Caparica, Portugal.
UCIBIO - Applied Molecular Biosciences Unit, Department of Chemistry, NOVA School of Science and Technology, Universidade NOVA de Lisboa, Caparica, Portugal.

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