Elucidating mechanisms in haem copper oxidases: The high-affinity Q(H) binding site in quinol oxidase as studied by DONUT-HYSCORE spectroscopy and density functional theory

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dc.contributor.authorMacMillan, Fraser
dc.contributor.authorKacprzak, Sylwia
dc.contributor.authorHellwig, Petra
dc.contributor.authorGrimaldi, Stephane
dc.contributor.authorMichel, Hartmut
dc.contributor.authorKaupp, Martin
dc.date.accessioned2016-06-30T06:33:41Z
dc.date.available2016-06-30T06:33:41Z
dc.date.issued2011
dc.descriptionDieser Beitrag ist mit Zustimmung des Rechteinhabers aufgrund einer (DFG geförderten) Allianz- bzw. Nationallizenz frei zugänglich.de
dc.descriptionThis publication is with permission of the rights owner freely accessible due to an Alliance licence and a national licence (funded by the DFG, German Research Foundation) respectively.en
dc.description.abstractThe Cytochrome bo3 ubiquinol oxidase (QOX) from Escherichia coli (E. coli) contains a redox-active quinone, the so-called “high-affinity” QH quinone. The location of this cofactor and its binding site has yet to be accurately determined by X-ray crystallographic studies. Based on site-directed mutagenesis studies, a putative quinone binding site in the protein has been proposed. The exact binding partner of this cofactor and also whether it is stabilised as an anionic semiquinone or as a neutral radical species is a matter of some speculation. Both Hyperfine Sub-level Correlation (HYSCORE) and Double Nuclear Coherence Transfer Spectroscopy (DONUT-HYSCORE) spectroscopy as well as density functional theory (DFT) have been applied to investigate the QH binding site in detail to resolve these issues. Use is made of site-directed variants as well as globally 15N/14N-exchanged protein. Comparison of computed and experimental 13C hyperfine tensors provides strong support for the binding of the semiquinone radical in an anionic rather than a neutral protonated form. These results are compared with the corresponding information available on other protein binding sites and/or on model systems and are discussed with regard to the location and potential function of QH in the overall mechanism of function of this family of haem copper oxidases.en
dc.description.sponsorshipDFG, SFB 472, Molekulare Bioenergetiken
dc.identifier.eissn1364-5498
dc.identifier.issn1359-6640
dc.identifier.pmid21322491
dc.identifier.urihttps://depositonce.tu-berlin.de/handle/11303/5740
dc.identifier.urihttp://dx.doi.org/10.14279/depositonce-5360
dc.language.isoen
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/en
dc.subject.ddc540 Chemie und zugeordnete Wissenschaftende
dc.titleElucidating mechanisms in haem copper oxidases: The high-affinity Q(H) binding site in quinol oxidase as studied by DONUT-HYSCORE spectroscopy and density functional theoryen
dc.typeArticleen
dc.type.versionpublishedVersionen
dcterms.bibliographicCitation.doi10.1039/c005149g
dcterms.bibliographicCitation.journaltitleFaraday discussionsen
dcterms.bibliographicCitation.originalpublishernameRoyal Society of Chemistryde
dcterms.bibliographicCitation.originalpublisherplaceCambridgede
dcterms.bibliographicCitation.pageend344
dcterms.bibliographicCitation.pagestart315
dcterms.bibliographicCitation.volume148
tub.accessrights.dnbdomain
tub.affiliationFak. 2 Mathematik und Naturwissenschaften::Inst. Chemiede
tub.affiliation.facultyFak. 2 Mathematik und Naturwissenschaftende
tub.affiliation.instituteInst. Chemiede
tub.publisher.universityorinstitutionTechnische Universität Berlin

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