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Thermodynamic and kinetic characterization of trihaem cytochrome c3 from Desulfuromonas acetoxidans

2002-10-28Journal article Restricted access
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dc.contributor.authorCorreia, Ilídio Joaquim Sobreira
dc.contributor.authorPaquete, Catarina
dc.contributor.authorLouro, Ricardo
dc.contributor.authorCatarino, Teresa
dc.contributor.authorTurner, David
dc.contributor.authorXavier, António
dc.date.accessioned2018-03-15T09:14:04Z
dc.date.available2018-03-15T09:14:04Z
dc.date.issued2002-10-28
dc.description.abstractTrihaem cytochrome c3 (also known as cytochrome c551.5 and cytochrome c7) is isolated from the periplasmic space of Desulfuromonas acetoxidans, a sulfur-reducing bacterium. Thermodynamic and kinetic data for the trihaem cytochrome c3 are presented and discussed in the context of the possible physiological implications of its functional properties with respect to the natural habitat of D. acetoxidans, namely as a symbiont with green sulfur bacteria working as a mini-sulfuretum. The thermodynamic properties were determined through the fit of redox titration data, followed by NMR and visible spectroscopy, to a model of four functional centres that describes the network of cooperativities between the three haems and one protolytic centre. The kinetics of trihaem cytochrome c3 reduction by sodium dithionite were studied using the stopped-flow technique and the data were fitted to a kinetic model that makes use of the thermodynamic properties to obtain the rate constants of the individual haems. This analysis indicates that the electrons enter the cytochrome mainly via haem I. The reduction potentials of the haems in this cytochrome show little variation with pH within the physiological range, and the kinetic studies show that the rates of reduction are also independent of pH in the range studied. Thus, although the trihaem cytochrome c3 is readily reduced by hydrogenases from Desulfovibrio sp. and its haem core is similar to that of the homologous tetrahaem cytochromes c3, its physico-chemical properties are quite different, which suggests that these multihaem cytochromes with similar structures perform different functions.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationCorreia, I.J., Paquete, C.M., Louro, R.O., Catarino, T., Turner, D.L. e Xavier, A.V. (2002) “Thermodynamic and kinetic characterisation of trihaem cytochrome c3 from Desulfuromonas acetoxidans”, European Journal of Biochemistry (FEBS Journal), Vol. 269(22), pp. 5722-5730pt_PT
dc.identifier.doi10.1046/j.1432-1033.2002.03286.xpt_PT
dc.identifier.urihttp://hdl.handle.net/10400.6/4617
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherWILEYpt_PT
dc.relationCytochrome c7: a haem protein with sulfur reductase activity
dc.relationStructural, Thermodynamic, and Kinetic Bases for Oxidative Phosphorylation in an Anaerobe: Desulfovibrio desulfuricans ATC 27774
dc.relationINTERAÇÃO DE HEMOPROTEÍNAS COM MOLÉCULAS ENVOLVIDAS EM TRANSDUÇÃO BIOQUÍMICA DE SINAIS
dc.relationESTUDOS MECANÍSTICOS, FUNCIONAIS E ESTRUTURAIS DE CITOCRÓMIOS MULTIHÉMICOS
dc.relation.publisherversionhttp://onlinelibrary.wiley.com/doi/10.1046/j.1432-1033.2002.03286.x/abstractpt_PT
dc.subjectCytochrome c7pt_PT
dc.subjectMultihaem cytochromespt_PT
dc.subjectRedox proteinspt_PT
dc.subjectThermodynamic and kinetic propertiespt_PT
dc.subjectTrihaem cytochrome c3pt_PT
dc.titleThermodynamic and kinetic characterization of trihaem cytochrome c3 from Desulfuromonas acetoxidanspt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleCytochrome c7: a haem protein with sulfur reductase activity
oaire.awardTitleStructural, Thermodynamic, and Kinetic Bases for Oxidative Phosphorylation in an Anaerobe: Desulfovibrio desulfuricans ATC 27774
oaire.awardTitleINTERAÇÃO DE HEMOPROTEÍNAS COM MOLÉCULAS ENVOLVIDAS EM TRANSDUÇÃO BIOQUÍMICA DE SINAIS
oaire.awardTitleESTUDOS MECANÍSTICOS, FUNCIONAIS E ESTRUTURAIS DE CITOCRÓMIOS MULTIHÉMICOS
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/POCI/POCTI%2FBIO%2F35699%2F2000/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/POCI/POCTI%2FBME%2F35021%2F2000/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/POCTI/SFRH%2FBPD%2F3585%2F2000/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT//PRAXIS XXI%2FBD%2F19870%2F99/PT
oaire.citation.endPage5730pt_PT
oaire.citation.startPage5722pt_PT
oaire.citation.titleEuropean Journal of Biochemistry (FEBS Journal)pt_PT
oaire.citation.volume269pt_PT
oaire.fundingStreamPOCI
oaire.fundingStreamPOCI
oaire.fundingStreamPOCTI
person.familyNameJoaquim Sobreira Correia
person.familyNamePaquete
person.familyNameLouro
person.familyNameCatarino
person.givenNameIlídio
person.givenNameCatarina
person.givenNameRicardo
person.givenNameTeresa
person.identifierUMbJ1KMAAAAJ
person.identifier.ciencia-idF610-7373-DC81
person.identifier.ciencia-idA01E-576D-43B7
person.identifier.ciencia-id641F-7315-F5CF
person.identifier.orcid0000-0003-1613-9675
person.identifier.orcid0000-0002-1511-3732
person.identifier.orcid0000-0002-2392-6450
person.identifier.orcid0000-0003-3782-4014
person.identifier.ridA-6615-2016
person.identifier.ridA-9267-2012
person.identifier.scopus-author-id7003557499
person.identifier.scopus-author-id6507206247
person.identifier.scopus-author-id6603724134
person.identifier.scopus-author-id6603075196
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.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
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsclosedAccesspt_PT
rcaap.typearticlept_PT
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