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Electron transfer in an acidophilic bacterium: interaction between a diheme cytochrome and a cupredoxin

dc.rights.licenseopenen_US
dc.contributor.authorWANG, X.
dc.contributor.authorROGER, M.
dc.contributor.authorCLEMENT, R.
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorLECOMTE, Sophie
dc.contributor.authorBIASO, F.
dc.contributor.authorABRIATA, L. A.
dc.contributor.authorMANSUELLE, P.
dc.contributor.authorMAZURENKO, I.
dc.contributor.authorGIUDICI-ORTICONI, M. T.
dc.contributor.authorLOJOU, E.
dc.contributor.authorILBERT, M.
dc.date.accessioned2020-04-07T13:48:05Z
dc.date.available2020-04-07T13:48:05Z
dc.date.issued2018
dc.identifier.issn2041-6520en_US
dc.identifier.otherhttp://www.rsc.org/suppdata/c8/sc/c8sc01615a/c8sc01615a1.pdfen_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/4152
dc.description.abstractEnAcidithiobacillus ferrooxidans, a chemolithoautotrophic Gram-negative bacterium, has a remarkable ability to obtain energy from ferrous iron oxidation at pH 2. Several metalloproteins have been described as being involved in this respiratory chain coupling iron oxidation with oxygen reduction. However, their properties and physiological functions remain largely unknown, preventing a clear understanding of the global mechanism. In this work, we focus on two metalloproteins of this respiratory pathway, a diheme cytochrome c(4) (Cyt c(4)) and a green copper protein (AcoP) of unknown function. We first demonstrate the formation of a complex between these two purified proteins, which allows homogeneous intermolecular electron-transfer in solution. We then mimic the physiological interaction between the two partners by replacing one at a time with electrodes displaying different chemical functionalities. From the electrochemical behavior of individual proteins, we show that, while electron transfer on AcoP requires weak electrostatic interaction, electron transfer on Cyt c(4) tolerates different charge and hydrophobicity conditions, suggesting a pivotal role of this protein in the metabolic chain. The electrochemical study of the proteins incubated together demonstrates an intermolecular electron transfer involving the protein complex, in which AcoP is reduced through the high potential heme of Cyt c(4). Modelling of the electrochemical signals at different scan rates allows us to estimate the rate constant of this intermolecular electron transfer in the range of a few s(-1). Possible routes for electron transfer in the acidophilic bacterium are deduced.
dc.description.sponsorshipBases moléculaires de l’immobilisation fonctionnelle d'enzymes pour des biopiles performantes - ANR-16-CE05-0024en_US
dc.language.isoENen_US
dc.title.enElectron transfer in an acidophilic bacterium: interaction between a diheme cytochrome and a cupredoxin
dc.title.alternativeChem. Sci.en_US
dc.typeArticle de revueen_US
dc.identifier.doi10.1039/c8sc01615a
dc.subject.halChimie/Matériauxen_US
bordeaux.journalChemical Scienceen_US
bordeaux.page4879-4891en_US
bordeaux.volume9en_US
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248
bordeaux.issue21en_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
hal.identifierhal-03160402
hal.version1
hal.date.transferred2021-03-05T09:50:17Z
hal.exporttrue
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