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Biochemical characterization of AniA from Neisseria gonorrhoeae

2022-04-07Outro Acesso aberto
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dc.contributor.authorBarreiro, Daniela Sofia Colaço
dc.contributor.authorOliveira, Ricardo
dc.contributor.authorPauleta, Sofia Rocha
dc.contributor.institutionDQ - Departamento de Química
dc.contributor.institutionUCIBIO - Applied Molecular Biosciences Unit
dc.date.accessioned2022-08-24T22:19:50Z
dc.date.available2022-08-24T22:19:50Z
dc.date.issued2022-04-07
dc.descriptionLA/P/0140/2020 PTDC/BIA PRO/109796/2009
dc.description.abstractAniA, the nitrite reductase from Neisseria gonorrhoeae, has been shown to play a crucial role in the infection mechanism of this microorganism by producing NO and abolishing epithelial exfoliation. This enzyme is a trimer with one type-1 copper center per subunit and one type-2 copper center in the subunits interface, with the latter being the catalytic site. The two centers were characterized by visible, EPR and CD spectroscopy for the first time, indicating that AniA's type-1 copper center has a high rhombicity, which is attributed to its tetrahedral geometry, and shorter Met-Cu bond, while type-2 copper center has the usual properties, though with a shorter hyperfine coupling constant (A//= 9.1 mT). The thermostability of AniA was analyzed by differential scanning calorimetry showing a single endothermic transition on the thermogram, with a maximum at 95 °C, while the CD spectra in the visible region indicates the presence of copper centers at 85-90 °C. The reoxidation rates of AniA in the presence of nitrite were analyzed by visible spectroscopy showing a pH dependence and being higher at pH 6.0. The high thermostability of this enzyme might be important for maintaining a high activity in the extracellular space and be less prone to denaturation and proteolysis.en
dc.description.versionpreprint
dc.description.versionpublished
dc.format.extent24
dc.format.extent1915177
dc.identifier.doi10.1101/2022.04.07.487406
dc.identifier.otherPURE: 45586117
dc.identifier.otherPURE UUID: efc97ad2-1cb0-4d9a-97b9-697376fe0e64
dc.identifier.otherORCID: /0000-0002-2149-9416/work/111168657
dc.identifier.urihttp://hdl.handle.net/10362/143280
dc.language.isoeng
dc.peerreviewedno
dc.relationinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDP%2F04378%2F2020/PT
dc.relationApplied Molecular Biosciences Unit
dc.relationApplied Molecular Biosciences Unit
dc.relationinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FBIA-BQM%2F29442%2F2017/PT
dc.relationBiochemical and functional characterization of enzymes from Neisseria gonorrhoeae and Staphylococcus aureus involved in the infection process
dc.relationinfo:eu-repo/grantAgreement/FCT/OE/UI%2FBD%2F151168%2F2021/PT
dc.subjectCopper nitrite reductase
dc.subjectNeisseria
dc.subjectspectroscopy
dc.subjectCopper enzyme
dc.subjectNitrite reduction
dc.subjectthermostability
dc.titleBiochemical characterization of AniA from Neisseria gonorrhoeaeen
dc.typeother
dspace.entity.typePublication
oaire.awardNumberUIDP/04378/2020
oaire.awardNumberUIDB/04378/2020
oaire.awardNumberPTDC/BIA-BQM/29442/2017
oaire.awardNumberUI/BD/151168/2021
oaire.awardTitleApplied Molecular Biosciences Unit
oaire.awardTitleApplied Molecular Biosciences Unit
oaire.awardTitleBiochemical and functional characterization of enzymes from Neisseria gonorrhoeae and Staphylococcus aureus involved in the infection process
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDP%2F04378%2F2020/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F04378%2F2020/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FBIA-BQM%2F29442%2F2017/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/OE/UI%2FBD%2F151168%2F2021/PT
oaire.fundingStream6817 - DCRRNI ID
oaire.fundingStream6817 - DCRRNI ID
oaire.fundingStream3599-PPCDT
oaire.fundingStreamOE
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.rightsrestrictedAccess
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