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Electron Flow From the Inner Membrane Towards the Cell Exterior in Geobacter sulfurreducens

2022-05-10Artigo científico Acesso aberto
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dc.contributor.authorAntunes, Jorge M. A.
dc.contributor.authorSilva, Marta A.
dc.contributor.authorSalgueiro, Carlos A.
dc.contributor.authorMorgado, Leonor
dc.contributor.institutionDQ - Departamento de Química
dc.contributor.institutionUCIBIO - Applied Molecular Biosciences Unit
dc.contributor.pblFrontiers Research Foundation
dc.date.accessioned2022-09-15T22:38:10Z
dc.date.available2022-09-15T22:38:10Z
dc.date.issued2022-05-10
dc.descriptionproject LA/P/0140/2020 (i4HB). Publisher Copyright: Copyright © 2022 Antunes, Silva, Salgueiro and Morgado.
dc.description.abstractExoelectrogenic microorganisms are in the spotlight due to their unique respiratory mechanisms and potential applications in distinct biotechnological fields, including bioremediation, bioenergy production and microbial electrosynthesis. These applications rely on the capability of these microorganisms to perform extracellular electron transfer, a mechanism that allows the bacteria to transfer electrons to the cell’s exterior by establishing functional interfaces between different multiheme cytochromes at the inner membrane, periplasmic space, and outer membrane. The multiheme cytochrome CbcL from Geobacter sulfurreducens is associated to the inner membrane and plays an essential role in the transfer of electrons to final electron acceptors with a low redox potential, as Fe(III) oxides and electrodes poised at −100 mV. CbcL has a transmembranar di-heme b-type cytochrome domain with six helices, linked to a periplasmic cytochrome domain with nine c-type heme groups. The complementary usage of ultraviolet-visible, circular dichroism and nuclear magnetic resonance permitted the structural and functional characterization of CbcL’s periplasmic domain. The protein was found to have a high percentage of disordered regions and its nine hemes are low-spin and all coordinated by two histidine residues. The apparent midpoint reduction potential of the CbcL periplasmic domain was determined, suggesting a thermodynamically favorable transfer of electrons to the putative redox partner in the periplasm − the triheme cytochrome PpcA. The establishment of a redox complex between the two proteins was confirmed by probing the electron transfer reaction and the molecular interactions between CbcL and PpcA. The results obtained show for the first time how electrons are injected into the periplasm of Geobacter sulfurreducens for subsequent transfer to the cell’s exterior.en
dc.description.versionpublishersversion
dc.description.versionpublished
dc.format.extent11
dc.format.extent1157830
dc.identifier.doi10.3389/fmicb.2022.898015
dc.identifier.issn1664-302X
dc.identifier.otherPURE: 46297239
dc.identifier.otherPURE UUID: e0ba8613-8b8f-4eac-b740-35105115ee25
dc.identifier.otherScopus: 85130680739
dc.identifier.otherWOS: 000803982500001
dc.identifier.otherPubMed: 35620088
dc.identifier.otherPubMedCentral: PMC9129911
dc.identifier.otherORCID: /0000-0002-3760-5180/work/119096702
dc.identifier.urihttp://hdl.handle.net/10362/143758
dc.identifier.urlhttps://www.scopus.com/pages/publications/85130680739
dc.language.isoeng
dc.peerreviewedyes
dc.relationFunding Information: info:eu-repo/grantAgreement/FCT/OE/SFRH%2FBPD%2F114848%2F2016/PT info:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FBIA-BQM%2F31981%2F2017/PT
dc.relationinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDP%2F04378%2F2020/PT
dc.relationApplied Molecular Biosciences Unit
dc.relationApplied Molecular Biosciences Unit
dc.relationPortuguese Nuclear Magnetic Resonance Network
dc.subjectextracellular electron transfer
dc.subjectGeobacter
dc.subjectinner membrane associated cytochrome
dc.subjectNMR
dc.subjectprotein-protein interactions
dc.subjectMicrobiology
dc.subjectMicrobiology (medical)
dc.titleElectron Flow From the Inner Membrane Towards the Cell Exterior in Geobacter sulfurreducensen
dc.title.subtitleBiochemical Characterization of Cytochrome CbcLen
dc.typejournal article
degois.publication.firstPage1
degois.publication.lastPage11
degois.publication.titleFrontiers in Microbiology
degois.publication.volume13
dspace.entity.typePublication
oaire.awardNumberUIDP/04378/2020
oaire.awardNumberUIDB/04378/2020
oaire.awardNumberPINFRA/22161/2016
oaire.awardTitleApplied Molecular Biosciences Unit
oaire.awardTitleApplied Molecular Biosciences Unit
oaire.awardTitlePortuguese Nuclear Magnetic Resonance Network
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDP%2F04378%2F2020/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F04378%2F2020/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/9444 - RNIIIE/PINFRA%2F22161%2F2016/PT
oaire.fundingStream6817 - DCRRNI ID
oaire.fundingStream6817 - DCRRNI ID
oaire.fundingStream9444 - RNIIIE
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccess
relation.isProjectOfPublication38373452-5c9c-4724-8def-f03314ecce0e
relation.isProjectOfPublicatione07cf232-4705-4b5b-b2c4-af8f25311076
relation.isProjectOfPublication9397b07c-a4e0-45e3-89ad-15ccd4ce1dec
relation.isProjectOfPublication.latestForDiscovery9397b07c-a4e0-45e3-89ad-15ccd4ce1dec

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