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The Neisseria gonorrhoeae cytochrome c2-bacterial peroxidase electron-transfer complex is competent in hydrogen peroxide reduction

2026-03Artigo científico Acesso aberto
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dc.contributor.authorBragança, Pedro M. S.
dc.contributor.authorBarreiro, Daniela S.
dc.contributor.authorCarepo, Marta S. P.
dc.contributor.authorPauleta, Sofia R.
dc.contributor.institutionDQ - Departamento de Química
dc.contributor.institutionUCIBIO - Applied Molecular Biosciences Unit
dc.contributor.institutionLAQV@REQUIMTE
dc.contributor.pblElsevier
dc.date.accessioned2026-02-27T12:49:01Z
dc.date.available2026-02-27T12:49:01Z
dc.date.issued2026-03
dc.descriptionPublisher Copyright: © 2025 The Authors. Published by Elsevier Inc. This is an open access article under the CC BY-NC-ND license. http://creativecommons.org/licenses/by-nc-nd/4.0/
dc.description.abstractNeisseria gonorrhoeae is a pathogenic bacterium responsible for the disease gonorrhea, which has gained increasing attention in recent years due to the emergence of strains resistant to the currently used antibiotics. In the absence of a vaccine, understanding mechanisms that contribute to infection is imperative. One such mechanism is the reduction of hydrogen peroxide by the outer membrane bound bacterial peroxidase. Here, steady-state kinetics shows that cytochrome c2, previously implicated in nitrite reduction, is an efficient electron donor to this enzyme, proving to be an alternative to the lipid-modified azurin. The cytochrome c2-mediated peroxidase activity has a KM of 0.74 ± 0.08 μM and a kobs of 18 ± 1 s−1for hydrogen peroxide, with an optimum pH at 7.7. The pH and ionic-strength dependence of this activity differs from that of azurin, suggesting that the two electron donors can play complementary roles depending on external conditions. Furthermore, the viscosity dependence of the activity suggests that protein-protein interactions are not purely diffusion-controlled but also governed by conformational changes required for complex formation and/or electron transfer, and docking analysis implies that cytochrome c2 binds near the exposed edge of the electron transferring heme of the bacterial peroxidase.This study improves our understanding of the periplasmic physiology of N. gonorrhoeae by demonstrating how the pathogen's flexibility in using electron donors enables it to maintain peroxidase activity and cope with oxidative stress in different host environments. These insights could inform future strategies aimed at disrupting redox homeostasis to combat antibiotic-resistant strains.en
dc.description.versionpublishersversion
dc.description.versionpublished
dc.format.extent9
dc.format.extent6741424
dc.identifier.doi10.1016/j.jinorgbio.2025.113164
dc.identifier.issn0162-0134
dc.identifier.otherPURE: 155171250
dc.identifier.otherPURE UUID: 72cd8ce2-7052-43ef-bf63-25197f4f4d59
dc.identifier.otherScopus: 105024962916
dc.identifier.otherPubMed: 41317563
dc.identifier.otherWOS: 001632037400001
dc.identifier.otherORCID: /0000-0002-2149-9416/work/206983122
dc.identifier.urihttp://hdl.handle.net/10362/200739
dc.identifier.urlhttps://www.scopus.com/pages/publications/105024962916
dc.identifier.urlhttps://www.webofscience.com/wos/woscc/full-record/WOS:001632037400001
dc.language.isoeng
dc.peerreviewedyes
dc.subjectBacterial peroxidase
dc.subjectc-type cytochrome
dc.subjectElectron-transfer complex
dc.subjectNeisseria gonorrhoeae
dc.subjectReactive oxygen species
dc.subjectSteady-state kinetics
dc.subjectBiochemistry
dc.subjectInorganic Chemistry
dc.subjectSDG 3 - Good Health and Well-being
dc.titleThe Neisseria gonorrhoeae cytochrome c2-bacterial peroxidase electron-transfer complex is competent in hydrogen peroxide reductionen
dc.typejournal article
degois.publication.firstPage1
degois.publication.lastPage9
degois.publication.titleJournal of Inorganic Biochemistry
degois.publication.volume276
dspace.entity.typePublication
rcaap.rightsopenAccess

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