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Thermodynamic characterization of a tetrahaem cytochrome isolated from a facultative aerobic bacterium, Shewanella frigidimarina: a putative redox model for flavocytochrome c3

dc.contributor.authorPessanha, Miguel
dc.contributor.authorLouro, Ricardo
dc.contributor.authorCorreia, Ilídio Joaquim Sobreira
dc.contributor.authorRothery, Emma
dc.contributor.authorPankhurst, Kate
dc.contributor.authorReid, Graeme
dc.contributor.authorChapman, Stephen
dc.contributor.authorTurner, David
dc.contributor.authorSalgueiro, Carlos
dc.date.accessioned2018-03-15T15:06:37Z
dc.date.available2018-03-15T15:06:37Z
dc.date.issued2003-03-01
dc.description.abstractThe facultative aerobic bacterium Shewanella frigidimarina produces a small c-type tetrahaem cytochrome (86 residues) under anaerobic growth conditions. This protein is involved in the respiration of iron and shares 42% sequence identity with the N-terminal domain of a soluble flavocytochrome, isolated from the periplasm of the same bacterium, which also contains four c-type haem groups. The thermodynamic properties of the redox centres and of an ionizable centre in the tetrahaem cytochrome were determined using NMR and visible spectroscopy techniques. This is the first detailed thermodynamic study performed on a tetrahaem cytochrome isolated from a facultative aerobic bacterium and reveals that this protein presents unique features. The redox centres have negative and different redox potentials, which are modulated by redox interactions between the four haems (covering a range of 8—56mV) and by redox—Bohr interactions between the haems and an ionizable centre (-4 to −36mV) located in close proximity to haem III. All of the interactions between the five centres are clearly dominated by electrostatic effects and the microscopic reduction potential of haem III is the one most affected by the oxidation of the other haems and by the protonation state of the molecule. Altogether, this study indicates that the tetrahaem cytochrome isolated from S. frigidimarina (Sfc) has the thermodynamic properties to work as an electron wire between its redox partners. Considering the high degree of sequence identity between Sfc and the cytochrome domain of flavocytochrome c3, the structural similarities of the haem core, and that the macroscopic potentials are also identical, the results obtained in this work are rationalized in order to put forward a putative redox model for flavocytochrome c3.pt_PT
dc.description.sponsorshipThis work was supported by a Fundac:a4o para a Cie#ncia e a Tecnologia (FCT)-Portugal grant (POCTI/QUI/42902/2001) and doctoral fellowship (SFRH/5229/2001), and by a Conselho de Reitores das Universidades Portuguesas (CRUP)-Portugal grant (B20/01, B32/02).
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationPessanha, M., Louro, R.O., Correia, I.J., Rothery, E.L., Pankhurst, K.L., Reid G.A., Chapman, S.K., Turner, D. L. e Salgueiro, C.A. (2003) “Thermodynamic characterization of a tetrahaem cytochrome isolated from a facultative aerobic bacterium, Shewanella frigidimarina: a putative redox model for flavocytochrome c3”, Biochemical Journal, Vol. 370, pp. 489-495pt_PT
dc.identifier.doi10.1042/bj20021408pt_PT
dc.identifier.urihttp://hdl.handle.net/10400.6/4619
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherPortland Presspt_PT
dc.relationStructural and functional mapping of a novel multihaem cytochrome: a model for fumarate reductases
dc.relation.publisherversionhttp://www.biochemj.org/content/370/2/489pt_PT
dc.subjectElectron transfer proteinpt_PT
dc.subjectMultihaempt_PT
dc.subjectNMRpt_PT
dc.subjectParamagnetic shiftpt_PT
dc.titleThermodynamic characterization of a tetrahaem cytochrome isolated from a facultative aerobic bacterium, Shewanella frigidimarina: a putative redox model for flavocytochrome c3pt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleStructural and functional mapping of a novel multihaem cytochrome: a model for fumarate reductases
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/POCI/POCTI%2FQUI%2F42902%2F2001/PT
oaire.citation.endPage495pt_PT
oaire.citation.startPage489pt_PT
oaire.citation.titleBiochemical Journalpt_PT
oaire.citation.volume370pt_PT
oaire.fundingStreamPOCI
person.familyNameLouro
person.familyNameJoaquim Sobreira Correia
person.givenNameRicardo
person.givenNameIlídio
person.identifierUMbJ1KMAAAAJ
person.identifier.ciencia-idF610-7373-DC81
person.identifier.orcid0000-0002-2392-6450
person.identifier.orcid0000-0003-1613-9675
person.identifier.scopus-author-id6603724134
person.identifier.scopus-author-id7003557499
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsclosedAccesspt_PT
rcaap.typearticlept_PT
relation.isAuthorOfPublication773007f7-2373-4bc9-87bc-a8acb3cc6309
relation.isAuthorOfPublicationf2c3e779-34a2-4309-950a-80687664c6ad
relation.isAuthorOfPublication.latestForDiscoveryf2c3e779-34a2-4309-950a-80687664c6ad
relation.isProjectOfPublicationccfbb42e-ce79-4827-b387-742770038664
relation.isProjectOfPublication.latestForDiscoveryccfbb42e-ce79-4827-b387-742770038664

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