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The solution structure of the soluble form of the lipid-modified azurin from Neisseria gonorrhoeae, the electron donor of cytochrome c peroxidase

2016-02Artigo científico Acesso aberto
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dc.contributor.authorNobrega, Claudia S.
dc.contributor.authorSaraiva, Ivo H.
dc.contributor.authorCarreira, Cintia
dc.contributor.authorDevreese, Bart
dc.contributor.authorMatzapetakis, Manolis
dc.contributor.authorPauleta, Sofia R.
dc.contributor.institutionMolecular, Structural and Cellular Microbiology (MOSTMICRO)
dc.contributor.institutionInstituto de Tecnologia Química e Biológica António Xavier (ITQB)
dc.contributor.institutionDQ - Departamento de Química
dc.contributor.institutionUCIBIO - Applied Molecular Biosciences Unit
dc.contributor.pblElsevier BV
dc.date.accessioned2018-05-02T22:05:11Z
dc.date.available2018-05-02T22:05:11Z
dc.date.issued2016-02
dc.descriptionWe thank Fundacao para a Ciencia e Tecnologia (FCT) for the financial support provided to SRP (PTDC/BIA-PRO/109796/2009), CSN (SFRH/BD/87878/2012) and IHS (SFRH/BPD/84404/2012), and that support the 600 MHz and 800 MHz NMR spectrometers that are part of the National NMR Network (RECI/BBB-BQB/0230/2012).
dc.description.abstractNeisseria gonorrhoeae colonizes the genitourinary track, and in these environments, especially in the female host, the bacteria are subjected to low levels of oxygen, and reactive oxygen and nitrosyl species. Here, the biochemical characterization of N. gonorrhoeae Laz is presented, as well as, the solution structure of its soluble domain determined by NMR N. gonorrhoeae Laz is a type 1 copper protein of the azurin-family based on its spectroscopic properties and structure, with a redox potential of 277 +/- 5 mV, at pH 7.0, that behaves as a monomer in solution. The globular Laz soluble domain adopts the Greek-key motif, with the copper center located at one end of the beta-barrel coordinated by Gly48, His49, Cys113, His118 and Met122, in a distorted trigonal geometry. The edge of the His118 imidazole ring is water exposed, in a surface that is proposed to be involved in the interaction with its redox partners. The heterologously expressed Laz was shown to be a competent electron donor to N. gonorrhoeae cytochrome c peroxidase. This is an evidence for its involvement in the mechanism of protection against hydrogen peroxide generated by neighboring lactobacilli in the host environment. (C) 2015 Elsevier B.V. All rights reserved.en
dc.description.versionpublishersversion
dc.description.versionpublished
dc.format.extent8
dc.format.extent766251
dc.identifier.doi10.1016/j.bbabio.2015.11.006
dc.identifier.issn0005-2728
dc.identifier.otherPURE: 1910384
dc.identifier.otherPURE UUID: a4a5b381-a447-4ccc-865d-56163f7293fc
dc.identifier.otherWOS: 000368204400005
dc.identifier.otherScopus: 84954119984
dc.identifier.otherPubMed: 26589091
dc.identifier.otherORCID: /0000-0002-2149-9416/work/55386523
dc.identifier.urihttp://hdl.handle.net/10362/35835
dc.language.isoeng
dc.peerreviewedyes
dc.subjectNeisseria
dc.subjectCopper protein
dc.subjectAzurin
dc.subjectLaz
dc.subjectCytochrome c peroxidase
dc.subjectSolution NMR structure
dc.subjectBLUE COPPER PROTEINS
dc.subjectPARACOCCUS-PANTOTROPHUS PSEUDOAZURIN
dc.subjectPSEUDOMONAS-AERUGINOSA AZURIN
dc.subjectOUTER-MEMBRANE PROTEIN
dc.subjectALCALIGENES-DENITRIFICANS
dc.subjectRESOLUTION STRUCTURE
dc.subjectACTIVE-SITES
dc.subjectH.8 EPITOPE
dc.subjectNMR SYSTEM
dc.subjectPLASTOCYANIN
dc.titleThe solution structure of the soluble form of the lipid-modified azurin from Neisseria gonorrhoeae, the electron donor of cytochrome c peroxidaseen
dc.typejournal article
degois.publication.firstPage169
degois.publication.issue2
degois.publication.lastPage176
degois.publication.titleBiochimica et Biophysica Acta-Bioenergetics
degois.publication.volume1857
dspace.entity.typePublication
rcaap.rightsopenAccess

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