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YhjA - An Escherichia coli trihemic enzyme with quinol peroxidase activity

2018-06Artigo científico Acesso aberto
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dc.contributor.authorNóbrega, Cláudia S.
dc.contributor.authorDevreese, Bart
dc.contributor.authorPauleta, Sofia R.
dc.contributor.institutionUCIBIO - Applied Molecular Biosciences Unit
dc.contributor.institutionDQ - Departamento de Química
dc.contributor.pblElsevier BV
dc.date.accessioned2021-02-16T23:18:29Z
dc.date.available2021-02-16T23:18:29Z
dc.date.issued2018-06
dc.descriptionBelgian Federal Science Policy Office (Belspo) (grant to BD, IAP7/44, iPROS project). co-financed by the ERDF under the PT2020 Partnership Agreement (POCI-01-0145-FEDER-007728).
dc.description.abstractThe trihemic bacterial cytochrome c peroxidase from Escherichia coli, YhjA, is a membrane-anchored protein with a C-terminal domain homologous to the classical bacterial peroxidases and an additional N-terminal (NT) heme binding domain. Recombinant YhjA is a 50 kDa monomer in solution with three c-type hemes covalently bound. Here is reported the first biochemical and spectroscopic characterization of YhjA and of the NT domain demonstrating that NT heme is His63/Met125 coordinated. The reduction potentials of P (active site), NT and E hemes were established to be −170 mV, +133 mV and +210 mV, respectively, at pH 7.5. YhjA has quinol peroxidase activity in vitro with optimum activity at pH 7.0 and millimolar range KM values using hydroquinone and menadiol (a menaquinol analogue) as electron donors (KM = 0.6 ± 0.2 and 1.8 ± 0.5 mM H2O2, respectively), with similar turnover numbers (kcat = 19 ± 2 and 13 ± 2 s−1, respectively). YhjA does not require reductive activation for maximum activity, in opposition to classical bacterial peroxidases, as P heme is always high-spin 6-coordinated with a water-derived molecule as distal axial ligand but shares the need for the presence of calcium ions in the kinetic assays. Formation of a ferryl Fe(IV) = O species was observed upon incubation of fully oxidized YhjA with H2O2. The data reported improve our understanding of the biochemical properties and catalytic mechanism of YhjA, a three-heme peroxidase that uses the quinol pool to defend the cells against hydrogen peroxide during transient exposure to oxygenated environments.en
dc.description.versionpublishersversion
dc.description.versionpublished
dc.format.extent12
dc.format.extent1362181
dc.identifier.doi10.1016/j.bbabio.2018.03.008
dc.identifier.issn0005-2728
dc.identifier.otherPURE: 3879091
dc.identifier.otherPURE UUID: c7fe18c8-11b8-4bba-88ba-16f91c135c74
dc.identifier.otherScopus: 85044124183
dc.identifier.otherPubMed: 29550214
dc.identifier.otherWOS: 000431160500001
dc.identifier.otherORCID: /0000-0002-2149-9416/work/88881747
dc.identifier.urihttp://hdl.handle.net/10362/111951
dc.identifier.urlhttps://www.scopus.com/pages/publications/85044124183
dc.language.isoeng
dc.peerreviewedyes
dc.relationinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/109796/PT
dc.relationInsights into novel bacterial cytochrome c peroxidases from pathogenic bacteria, Neisseria gonorrhoeae and Escherichia coli
dc.relationinfo:eu-repo/grantAgreement/FCT/5876/147258/PT
dc.subjectEscherichia coli
dc.subjectHeme enzyme
dc.subjectOxidative stress
dc.subjectQuinol peroxidase activity
dc.subjectTrihemic bacterial peroxidase
dc.subjectBiophysics
dc.subjectBiochemistry
dc.subjectCell Biology
dc.titleYhjA - An Escherichia coli trihemic enzyme with quinol peroxidase activityen
dc.typejournal article
degois.publication.firstPage411
degois.publication.issue6
degois.publication.lastPage422
degois.publication.titleBiochimica et Biophysica Acta - Bioenergetics
degois.publication.volume1859
dspace.entity.typePublication
oaire.awardNumberPTDC/BIA-PRO/109796/2009
oaire.awardNumberSFRH/BD/87878/2012
oaire.awardNumberUID/Multi/04378/2013
oaire.awardTitleInsights into novel bacterial cytochrome c peroxidases from pathogenic bacteria, Neisseria gonorrhoeae and Escherichia coli
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FBIA-PRO%2F109796%2F2009/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/SFRH/SFRH%2FBD%2F87878%2F2012/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/5876/UID%2FMulti%2F04378%2F2013/PT
oaire.fundingStream3599-PPCDT
oaire.fundingStreamSFRH
oaire.fundingStream5876
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
rcaap.rightsopenAccess
relation.isProjectOfPublicationcd0ae1eb-f3c0-4c2a-a494-545b1f30478b
relation.isProjectOfPublicationfe8e8e77-40e8-40fb-9fc4-9f27f8c240a9
relation.isProjectOfPublicationf6c6102f-c577-4633-a70c-08a0b27e1207
relation.isProjectOfPublication.latestForDiscoveryf6c6102f-c577-4633-a70c-08a0b27e1207

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