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Unveiling the membrane bound dihydroorotate

2023-04-01Artigo científico Acesso aberto
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dc.contributor.authorSousa, Filipe M.
dc.contributor.authorPires, Patrícia
dc.contributor.authorBarreto, Andreia
dc.contributor.authorRefojo, Patrícia N.
dc.contributor.authorSilva, Micael S.
dc.contributor.authorFernandes, Pedro B.
dc.contributor.authorCarapeto, Ana P.
dc.contributor.authorRobalo, Tiago T.
dc.contributor.authorRodrigues, Mário S.
dc.contributor.authorPinho, Mariana G.
dc.contributor.authorCabrita, Eurico J.
dc.contributor.authorPereira, Manuela M.
dc.contributor.institutionInstituto de Tecnologia Química e Biológica António Xavier (ITQB)
dc.contributor.institutionUCIBIO - Applied Molecular Biosciences Unit
dc.contributor.institutionDQ - Departamento de Química
dc.contributor.institutionFaculdade de Ciências e Tecnologia (FCT)
dc.contributor.pblElsevier BV
dc.date.accessioned2023-10-03T22:19:19Z
dc.date.available2023-10-03T22:19:19Z
dc.date.issued2023-04-01
dc.descriptionFunding Information: Helena Gaspar is acknowledged for the HPLC analyses and Bruno Victor for advice on modelling. F.M.S. and M.S.S. are recipients of fellowships by Fundação para a Ciência e a Tecnologia (PD/BD/128213/2016 and PD/BD/128202/2016, respectively, both within the scope of the PhD program Molecular Biosciences PD/00133/2012). A.B. is recipient of a fellowship by Fundação para a Ciência e a Tecnologia UI/BD/153052/2022. The work was funded by Fundação para a Ciência e a Tecnologia ( PTDC/BIA-BQM/2599/2021 to M.M.P). The project was further supported by UIDB/04046/2020 and UIDP/04046/2020 Centre grants from FCT , Portugal (to BioISI), by LISBOA-01-0145-FEDER-007660 cofunded by FEDER through COMPETE2020-POCI and by Fundação para a Ciência e a Tecnologia and by UIDB/04612/2020 and UIDP/04612/2020 research unit grants from FCT (to Mostmicro). The NMR spectrometers are part of the National NMR Network (PTNMR) and are supported by Infrastructure Project N° 022161 (co-financed by FEDER through COMPETE 2020, POCI, and PORL and FCT through PIDDAC). Funding Information: Helena Gaspar is acknowledged for the HPLC analyses and Bruno Victor for advice on modelling. F.M.S. and M.S.S. are recipients of fellowships by Fundação para a Ciência e a Tecnologia (PD/BD/128213/2016 and PD/BD/128202/2016, respectively, both within the scope of the PhD program Molecular Biosciences PD/00133/2012). A.B. is recipient of a fellowship by Fundação para a Ciência e a Tecnologia UI/BD/153052/2022. The work was funded by Fundação para a Ciência e a Tecnologia (PTDC/BIA-BQM/2599/2021 to M.M.P). The project was further supported by UIDB/04046/2020 and UIDP/04046/2020 Centre grants from FCT, Portugal (to BioISI), by LISBOA-01-0145-FEDER-007660 cofunded by FEDER through COMPETE2020-POCI and by Fundação para a Ciência e a Tecnologia and by UIDB/04612/2020 and UIDP/04612/2020 research unit grants from FCT (to Mostmicro). The NMR spectrometers are part of the National NMR Network (PTNMR) and are supported by Infrastructure Project N° 022161 (co-financed by FEDER through COMPETE 2020, POCI, and PORL and FCT through PIDDAC). Publisher Copyright: © 2022 The Author(s)
dc.description.abstractStaphylococcus aureus is an opportunistic pathogen and one of the most frequent causes for community acquired and nosocomial bacterial infections. Even so, its energy metabolism is still under explored and its respiratory enzymes have been vastly overlooked. In this work, we unveil the dihydroorotate:quinone oxidoreductase (DHOQO) from S. aureus, the first example of a DHOQO from a Gram-positive organism. This protein was shown to be a FMN containing menaquinone reducing enzyme, presenting a Michaelis-Menten behaviour towards the two substrates, which was inhibited by Brequinar, Leflunomide, Lapachol, HQNO, Atovaquone and TFFA with different degrees of effectiveness. Deletion of the DHOQO coding gene (Δdhoqo) led to lower bacterial growth rates, and effected in cell morphology and metabolism, most importantly in the pyrimidine biosynthesis, here systematized for S. aureus MW2 for the first time. This work unveils the existence of a functional DHOQO in the respiratory chain of the pathogenic bacterium S. aureus, enlarging the understanding of its energy metabolism.en
dc.description.versionpublishersversion
dc.description.versionpublished
dc.format.extent6523589
dc.identifier.doi10.1016/j.bbabio.2022.148948
dc.identifier.issn0005-2728
dc.identifier.otherPURE: 72696123
dc.identifier.otherPURE UUID: 04249556-89f7-4fec-b6a1-85f783e42e87
dc.identifier.otherScopus: 85145610605
dc.identifier.otherPubMed: 36481274
dc.identifier.urihttp://hdl.handle.net/10362/158656
dc.identifier.urlhttps://www.scopus.com/pages/publications/85145610605
dc.language.isoeng
dc.peerreviewedyes
dc.subjectBacterial respiration
dc.subjectDHODH
dc.subjectelectron transfer
dc.subjectFlavoprotein
dc.subjectFMN
dc.subjectQuinone
dc.subjectRespiratory chain
dc.subjectStaphylococcus aureus
dc.subjectBiophysics
dc.subjectBiochemistry
dc.subjectCell Biology
dc.titleUnveiling the membrane bound dihydroorotateen
dc.title.subtitleQuinone oxidoreductase from Staphylococcus aureusen
dc.typejournal article
degois.publication.issue2
degois.publication.titleBiochimica et Biophysica Acta - Bioenergetics
degois.publication.volume1864
dspace.entity.typePublication
rcaap.rightsopenAccess

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