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Proton-assisted Two-electron Transfer in Natural Variants of Tetraheme Cytochromes from Desulfomicrobium Sp.

2004-09-28Journal article Restricted access
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dc.contributor.authorCorreia, Ilídio Joaquim Sobreira
dc.contributor.authorPaquete, Catarina
dc.contributor.authorCoelho, Ana
dc.contributor.authorAlmeida, Claudia
dc.contributor.authorCatarino, Teresa
dc.contributor.authorLouro, Ricardo
dc.contributor.authorFrazão, Carlos
dc.contributor.authorSaraiva, Lígia M.
dc.contributor.authorCarrondo, Maria
dc.contributor.authorTurner, David
dc.contributor.authorXavier, António
dc.date.accessioned2018-03-15T15:30:51Z
dc.date.available2018-03-15T15:30:51Z
dc.date.issued2004-09-28
dc.description.abstractThe tetraheme cytochrome c3 isolated from Desulfomicrobium baculatum (DSM 1743)(Dsmb) was cloned, and the sequence analysis showed that this cytochrome differs in just three amino acid residues from the cytochrome c3 isolated from Desulfomicrobium norvegicum (Dsmn): (DsmnXXDsmb) Thr-37 → Ser, Val-45 → Ala, and Phe-88 → Tyr. X-ray crystallography was used to determine the structure of cytochrome c3 from Dsmb, showing that it is very similar to the published structure of cytochrome c3 from Dsmn. A detailed thermodynamic and kinetic characterization of these two tetraheme cytochromes c3 was performed by using NMR and visible spectroscopy. The results obtained show that the network of cooperativities between the redox and protonic centers is consistent with a synergetic process to stimulate the hydrogen uptake activity of hydrogenase. This is achieved by increasing the affinity of the cytochrome for protons through binding electrons and, reciprocally, by favoring a concerted two-electron transfer assisted by the binding of proton(s). The data were analyzed within the framework of the differences in the primary and tertiary structures of the two proteins, showing that residue 88, close to heme I, is the main cause for the differences in the microscopic thermodynamic parameters obtained for these two cytochromes c3. This comparison reveals how replacement of a single amino acid can tune the functional properties of energy-transducing proteins, so that they can be optimized to suit the bioenergetic constraints of specific habitats.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationCorreia, I.J., Paquete, C.M., Coelho, A., Almeida, C.C., Catarino, T., Louro, R.O., Frazão, C., Saraiva, L.M., Carrondo, M.A., Turner, D.L. e Xavier, A.V. (2004) “Proton-assisted two-electron transfer in natural variants of tetraheme cytochromes from Desulfomicrobium Sp.”, Journal of Biological Chemistry, Vol. 279 (50), pp. 52227-52237pt_PT
dc.identifier.doi10.1074/jbc.M408763200pt_PT
dc.identifier.urihttp://hdl.handle.net/10400.6/4620
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherAmerican Society for Biochemistry and Molecular Biologypt_PT
dc.relationStructural, Thermodynamic, and Kinetic Bases for Oxidative Phosphorylation in an Anaerobe: Desulfovibrio desulfuricans ATC 27774
dc.relationBinding of diatomic molecules to haem proteins
dc.relationCITOCROMO c COM 9 HEMOS DE DESULFOVIBRIO DESULFURICANS ATCC 27774: ANÁLISE TERMODINÂMICA, CINÉTICA E FUNCIONAL
dc.relationESTUDOS MECANÍSTICOS, FUNCIONAIS E ESTRUTURAIS DE CITOCRÓMIOS MULTIHÉMICOS
dc.relation.publisherversionhttp://www.jbc.org/content/279/50/52227.fullpt_PT
dc.subjectDesulfomicrobium Sp.pt_PT
dc.subjectCytochromespt_PT
dc.subjectNMRpt_PT
dc.titleProton-assisted Two-electron Transfer in Natural Variants of Tetraheme Cytochromes from Desulfomicrobium Sp.pt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleStructural, Thermodynamic, and Kinetic Bases for Oxidative Phosphorylation in an Anaerobe: Desulfovibrio desulfuricans ATC 27774
oaire.awardTitleBinding of diatomic molecules to haem proteins
oaire.awardTitleCITOCROMO c COM 9 HEMOS DE DESULFOVIBRIO DESULFURICANS ATCC 27774: ANÁLISE TERMODINÂMICA, CINÉTICA E FUNCIONAL
oaire.awardTitleESTUDOS MECANÍSTICOS, FUNCIONAIS E ESTRUTURAIS DE CITOCRÓMIOS MULTIHÉMICOS
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/POCI/POCTI%2FBME%2F35021%2F2000/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/POCI/POCTI%2FQUI%2F43435%2F2001/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/POCI-2010/SFRH%2FBD%2F6495%2F2001/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT//PRAXIS XXI%2FBD%2F19870%2F99/PT
oaire.citation.endPage52237pt_PT
oaire.citation.startPage52227pt_PT
oaire.citation.titleThe Journal of Biological Chemistrypt_PT
oaire.citation.volume279pt_PT
oaire.fundingStreamPOCI
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oaire.fundingStreamPOCI-2010
person.familyNameJoaquim Sobreira Correia
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person.familyNameAbreu Fonseca de Carvalho Teixeira Carrondo
person.familyNameTurner
person.givenNameIlídio
person.givenNameCatarina
person.givenNameAna
person.givenNameTeresa
person.givenNameRicardo
person.givenNameCarlos
person.givenNameLigia
person.givenNameMaria Arménia
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project.funder.identifierhttp://doi.org/10.13039/501100001871
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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.embargofctCopyright cedido à editora no momento da publicaçãopt_PT
rcaap.rightsclosedAccesspt_PT
rcaap.typearticlept_PT
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