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Structural Characterization of Neisseria gonorrhoeae Bacterial Peroxidase—Insights into the Catalytic Cycle of Bacterial Peroxidases

2023-03-26Artigo científico Acesso aberto
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dc.contributor.authorNóbrega, Cláudia S.
dc.contributor.authorCarvalho, Ana Luísa
dc.contributor.authorRomão, Maria João
dc.contributor.authorPauleta, Sofia R.
dc.contributor.institutionUCIBIO - Applied Molecular Biosciences Unit
dc.contributor.institutionDQ - Departamento de Química
dc.contributor.pblMDPI - Multidisciplinary Digital Publishing Institute
dc.date.accessioned2023-04-03T22:15:23Z
dc.date.available2023-04-03T22:15:23Z
dc.date.issued2023-03-26
dc.descriptionAcknowledgments The authors would like to thank Lina Juknaité for her contribution in the initial crystallization studies. The authors acknowledge the European Synchrotron Radiation Facility and the Swiss Light Source for provision of synchrotron radiation facilities and access to beamlines BM30 and PXIII (X06DA), respectively.
dc.description.abstractNeisseria gonorrhoeae is an obligate human pathogenic bacterium responsible for gonorrhea, a sexually transmitted disease. The bacterial peroxidase, an enzyme present in the periplasm of this bacterium, detoxifies the cells against hydrogen peroxide and constitutes one of the primary defenses against exogenous and endogenous oxidative stress in this organism. The 38 kDa heterologously produced bacterial peroxidase was crystallized in the mixed-valence state, the active state, at pH 6.0, and the crystals were soaked with azide, producing the first azide-inhibited structure of this family of enzymes. The enzyme binds exogenous ligands such as cyanide and azide, which also inhibit the catalytic activity by coordinating the P heme iron, the active site, and competing with its substrate, hydrogen peroxide. The inhibition constants were estimated to be 0.4 ± 0.1 µM and 41 ± 5 mM for cyanide and azide, respectively. Imidazole also binds and inhibits the enzyme in a more complex mechanism by binding to P and E hemes, which changes the reduction potential of the latest heme. Based on the structures now reported, the catalytic cycle of bacterial peroxidases is revisited. The inhibition studies and the crystal structure of the inhibited enzyme comprise the first platform to search and develop inhibitors that target this enzyme as a possible new strategy against N. gonorrhoeae.en
dc.description.versionpublishersversion
dc.description.versionpublished
dc.format.extent21
dc.format.extent4709411
dc.identifier.doi10.3390/ijms24076246
dc.identifier.issn1422-0067
dc.identifier.otherPURE: 57231711
dc.identifier.otherPURE UUID: 2830a808-c5d8-4cd5-b509-40e2c10dc7da
dc.identifier.othercrossref: 10.3390/ijms24076246
dc.identifier.otherScopus: 85152326254
dc.identifier.otherWOS: 000970051400001
dc.identifier.otherORCID: /0000-0002-3824-0240/work/132351334
dc.identifier.otherORCID: /0000-0002-3004-0543/work/132351387
dc.identifier.otherORCID: /0000-0002-2149-9416/work/132351469
dc.identifier.urihttp://hdl.handle.net/10362/151545
dc.language.isoeng
dc.peerreviewedyes
dc.relationinfo:eu-repo/grantAgreement/FCT/Concurso para Projectos de I&D em todos os Domínios Científicos - 2009/PTDC%2FBIA-PRO%2F109796%2F2009/PT
dc.relationinfo:eu-repo/grantAgreement/FCT/Concurso para Financiamento de Projetos de Investigação Científica e Desenvolvimento Tecnológico em Todos os Domínios Científicos - 2017/PTDC%2FBIA-BQM%2F29442%2F2017/PT
dc.relationDetoxification of Hydrogen Peroxide by Pathogenic Bacteria - E.coli Tri-haem peroxidase as a model
dc.relationModern Structural Biology: Resources for the advancement of in-house X-ray Crystallography
dc.relationBIOCHEMICAL AND PHYSIOLOGICAL INSIGHTS INTO THE BACTERIAL CYTOCHROME C PEROXIDASE FROM ESCHERICHIA COLI
dc.relationApplied Molecular Biosciences Unit
dc.relationApplied Molecular Biosciences Unit
dc.relationInstitute for Health and Bioeconomy
dc.relationinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F04378%2F2020/PT
dc.relationinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/LA%2FP%2F0140%2F2020/PT
dc.subjectBacterial peroxidase
dc.subjectpathogenic bacteria
dc.subjectNeisseria gonorrhoeae
dc.subjectinhibition
dc.subjectGeneral Agricultural and Biological Sciences
dc.subjectSDG 3 - Good Health and Well-being
dc.titleStructural Characterization of Neisseria gonorrhoeae Bacterial Peroxidase—Insights into the Catalytic Cycle of Bacterial Peroxidasesen
dc.typejournal article
degois.publication.issue7
degois.publication.titleInternational Journal of Molecular Sciences
degois.publication.volume24
dspace.entity.typePublication
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oaire.awardTitleDetoxification of Hydrogen Peroxide by Pathogenic Bacteria - E.coli Tri-haem peroxidase as a model
oaire.awardTitleModern Structural Biology: Resources for the advancement of in-house X-ray Crystallography
oaire.awardTitleBIOCHEMICAL AND PHYSIOLOGICAL INSIGHTS INTO THE BACTERIAL CYTOCHROME C PEROXIDASE FROM ESCHERICHIA COLI
oaire.awardTitleApplied Molecular Biosciences Unit
oaire.awardTitleApplied Molecular Biosciences Unit
oaire.awardTitleInstitute for Health and Bioeconomy
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