Reactivation from the Ni-B state in [NiFe] hydrogenase of Ralstonia eutropha is controlled by reduction of the superoxidised proximal cluster

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dc.contributor.authorRadu, Valentin
dc.contributor.authorFrielingsdorf, Stefan
dc.contributor.authorLenz, Oliver
dc.contributor.authorJeuken, Lars J. C.
dc.date.accessioned2017-10-24T07:15:45Z
dc.date.available2017-10-24T07:15:45Z
dc.date.issued2016
dc.description.abstractThe tolerance towards oxic conditions of O-2-tolerant [NiFe] hydrogenases has been attributed to an unusual [4Fe-3S] cluster that lies proximal to the [NiFe] active site. Upon exposure to oxygen, this cluster converts to a superoxidised (5+) state, which is believed to secure the formation of the so-called Ni-B state that is rapidly reactivated under reducing conditions. Here, the reductive reactivation of the membrane-bound [NiFe]-hydrogenase (MBH) from Ralstonia eutropha in a native-like lipid membrane was characterised and compared to a variant that instead carries a typical [4Fe-4S] proximal cluster. Reactivation from the Ni-B state was faster in the [4Fe-4S] variant, suggesting that the reactivation rate in MBH is limited by the reduction of the superoxidised [4Fe-3S] cluster. We propose that the [4Fe-3S] cluster plays a major role in protecting MBH by blocking the reversal of electron transfer to the [NiFe] active site, which would produce damaging radical oxygen species.en
dc.description.sponsorshipEC/FP7/280518/EU/Membrane-modified Electrodes to study Membrane Enzymes/MEMEen
dc.description.sponsorshipDFG, EXC 314, Unifying Concepts in Catalysisen
dc.identifier.eissn1364-548X
dc.identifier.issn1359-7345
dc.identifier.pmid26750202
dc.identifier.urihttps://depositonce.tu-berlin.de/handle/11303/6909
dc.identifier.urihttp://dx.doi.org/10.14279/depositonce-6248
dc.language.isoen
dc.rights.urihttps://creativecommons.org/licenses/by/3.0/
dc.subject.ddc540 Chemie und zugeordnete Wissenschaftende
dc.titleReactivation from the Ni-B state in [NiFe] hydrogenase of Ralstonia eutropha is controlled by reduction of the superoxidised proximal clusteren
dc.typeArticleen
dc.type.versionpublishedVersionen
dcterms.bibliographicCitation.doi10.1039/c5cc10382g
dcterms.bibliographicCitation.issue12
dcterms.bibliographicCitation.journaltitleChemical communicationsen
dcterms.bibliographicCitation.originalpublishernameRoyal Society of Chemistryde
dcterms.bibliographicCitation.originalpublisherplaceCambridgede
dcterms.bibliographicCitation.pageend2635
dcterms.bibliographicCitation.pagestart2632
dcterms.bibliographicCitation.volume52
tub.accessrights.dnbfree
tub.affiliationFak. 2 Mathematik und Naturwissenschaften::Inst. Chemie::FG Physikalische Chemie / Biophysikalische Chemiede
tub.affiliation.facultyFak. 2 Mathematik und Naturwissenschaftende
tub.affiliation.groupFG Physikalische Chemie / Biophysikalische Chemiede
tub.affiliation.instituteInst. Chemiede
tub.publisher.universityorinstitutionTechnische Universität Berlin

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