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Regulation of the mechanism of Type-II NADH: Quinone oxidoreductase from S. aureus

2018-06-01Artigo científico Acesso aberto
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dc.contributor.authorSena, Filipa V.
dc.contributor.authorSousa, Filipe M.
dc.contributor.authorOliveira, Ana Sofia F.
dc.contributor.authorSoares, Cláudio M.
dc.contributor.authorCatarino, Teresa
dc.contributor.authorPereira, Manuela M.
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.pblElsevier
dc.date.accessioned2019-04-02T22:14:33Z
dc.date.available2019-04-02T22:14:33Z
dc.date.issued2018-06-01
dc.descriptionPD/BD/113985/2015 PD/BD/128213/2016 PD/00133/2012 IF/01507/2015 LISBOA-01-0145-FEDER-007660 FVS and FMS are recipients of fellowships by Fundacao para a Ciencia e a Tecnologia (PD/BD/113985/2015, PD/BD/128213/2016, respectively (within the scope of the PhD program Molecular Biosciences PD/00133/2012)). The work was funded by Fundacao para a Ciencia e a Tecnologia (IF/01507/2015 to MMP). This work was also supported by Project LISBOA-01-0145-FEDER-007660 (Microbiologia Molecular, Estrutural e Celular) funded by FEDER funds through COMPETE2020 - Programa Operacional Competitividade e Internacionalizacao (POCI) and by national funds through FCT - Fundacao para a Ciencia e a Tecnologia and by national funds through FCT - Fundacao para a Ciencia e a Tecnologia and by UID/MULTI/04046/2013 centre grant from FCT, Portugal (to BioISI).
dc.description.abstractType-II NADH:quinone oxidoreductases (NDH-2s) are membrane proteins involved in respiratory chains and the only enzymes with NADH:quinone oxidoreductase activity expressed in Staphylococcus aureus (S. aureus), one of the most common causes of clinical infections. NDH-2s are members of the two-Dinucleotide Binding Domains Flavoprotein (tDBDF) superfamily, having a flavin adenine dinucleotide, FAD, as prosthetic group and NAD(P)H as substrate. The establishment of a Charge-Transfer Complex (CTC) between the isoalloxazine ring of the reduced flavin and the nicotinamide ring of NAD+ in NDH-2 was described, and in this work we explored its role in the kinetic mechanism using different electron donors and electron acceptors. We observed that CTC slows down the rate of the second half reaction (quinone reduction) and determines the effect of HQNO, an inhibitor. Also, protonation equilibrium simulations clearly indicate that the protonation probability of an important residue for proton transfer to the active site (D302) is influenced by the presence of the CTC. We propose that CTC is critical for the overall mechanism of NDH-2 and possibly relevant to keep a low quinol/quinone ratio and avoid excessive ROS production in vivo.en
dc.description.versionpublishersversion
dc.description.versionpublished
dc.format.extent6
dc.format.extent518089
dc.identifier.doi10.1016/j.redox.2018.02.004
dc.identifier.issn2213-2317
dc.identifier.otherPURE: 3910906
dc.identifier.otherPURE UUID: e6990101-26c4-4b0f-b80e-038674eb15e6
dc.identifier.otherScopus: 85042943505
dc.identifier.otherWOS: :000446404400020
dc.identifier.otherPubMed: 29524843
dc.identifier.otherPubMedCentral: PMC5857484
dc.identifier.otherORCID: /0000-0003-1154-556X/work/56430330
dc.identifier.urihttp://www.scopus.com/inward/record.url?scp=85042943505&partnerID=8YFLogxK
dc.identifier.urlhttps://www.scopus.com/pages/publications/85042943505
dc.language.isoeng
dc.peerreviewedyes
dc.relationinfo:eu-repo/grantAgreement/FCT/5876/147256/PT
dc.subjectBacterial respiration
dc.subjectElectron transfer
dc.subjectFAD
dc.subjectFlavoprotein
dc.subjectKinetics
dc.subjectRespiratory chain
dc.subjectBiochemistry
dc.subjectOrganic Chemistry
dc.titleRegulation of the mechanism of Type-II NADH: Quinone oxidoreductase from S. aureusen
dc.typejournal article
degois.publication.firstPage209
degois.publication.lastPage214
degois.publication.titleRedox Biology
degois.publication.volume16
dspace.entity.typePublication
oaire.awardNumberUID/Multi/04046/2013
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/5876/UID%2FMulti%2F04046%2F2013/PT
oaire.fundingStream5876
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccess
relation.isProjectOfPublication3e61392f-bdce-4abc-81ef-75d52877635f
relation.isProjectOfPublication.latestForDiscovery3e61392f-bdce-4abc-81ef-75d52877635f

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