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Arsenite oxidase in complex with antimonite and arsenite oxyanions

2023-08Artigo científico Acesso aberto
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dc.contributor.authorEngrola, Filipa
dc.contributor.authorCorreia, Márcia A.S.
dc.contributor.authorWatson, Cameron
dc.contributor.authorRomão, Carlos C.
dc.contributor.authorVeiros, Luis F.
dc.contributor.authorRomão, Maria João
dc.contributor.authorSantos-Silva, Teresa
dc.contributor.authorSantini, Joanne M.
dc.contributor.institutionUCIBIO - Applied Molecular Biosciences Unit
dc.contributor.institutionInstituto de Tecnologia Química e Biológica António Xavier (ITQB)
dc.contributor.pblASBMB - American Society for Biochemistry and Molecular Biology
dc.date.accessioned2023-10-03T22:19:55Z
dc.date.available2023-10-03T22:19:55Z
dc.date.issued2023-08
dc.descriptionFunding Information: Work supported by UCIBIO funding from FCT-MCTES ( UIDB/04378/2020 , UIDP/04378/2020 , and Engrola PhD student grant UI/BD/151155/2021 ) and the Institute for Health and Bioeconomy—i4HB (project LA/P/0140/2020 ). Centro de Química Estrutural (CQE) and Institute of Molecular Sciences (IMS) acknowledge the financial support of FCT-MCTES (Projects UIDB/00100/2020 , UIDP/00100/2020 , and LA/P/0056/2020 , respectively). The authors thank Doctor Pedro Matias for valuable discussions and acknowledge MAX IV Laboratory for time on Beamline Biomax under Proposal [ID20190007]. Research conducted at MAX IV is supported by the Swedish Research council under contract 2018-07152 , the Swedish Governmental Agency for Innovation Systems under contract 2018-04969 , and Formas under contract 2019-02496 . We also acknowledge the Paul Scherrer Institut, Villigen, Switzerland for synchrotron radiation beamtime at beamline PXIII. Some measurements were performed at XALOC beamline at ALBA Synchrotron with the collaboration of ALBA staff. Funding Information: C. W. is supported by a Biotechnology and Biological Sciences Research Council (BBSRC) Industrial CASE Studentship ( BB/L01615X/1 ) with Bio Nano Consulting Ltd as the industrial partner. Publisher Copyright: © 2023 The Authors
dc.description.abstractArsenic contamination of groundwater is among one of the biggest health threats affecting millions of people in the world. There is an urgent need for efficient arsenic biosensors where the use of arsenic metabolizing enzymes can be explored. In this work, we have solved four crystal structures of arsenite oxidase (Aio) in complex with arsenic and antimony oxyanions and the structures determined correspond to intermediate states of the enzymatic mechanism. These structural data were complemented with density-functional theory calculations providing a unique view of the molybdenum active site at different time points that, together with mutagenesis data, enabled to clarify the enzymatic mechanism and the molecular determinants for the oxidation of As(III) to the less toxic As(V) species.en
dc.description.versionpublishersversion
dc.description.versionpublished
dc.format.extent2452349
dc.identifier.doi10.1016/j.jbc.2023.105036
dc.identifier.issn0021-9258
dc.identifier.otherPURE: 72982040
dc.identifier.otherPURE UUID: e9ff0415-e00b-403b-8247-c3ba88a1e683
dc.identifier.otherScopus: 85167420000
dc.identifier.otherPubMed: 37442232
dc.identifier.otherORCID: /0000-0003-0636-8095/work/151387981
dc.identifier.otherORCID: /0000-0002-3004-0543/work/151421994
dc.identifier.urihttp://hdl.handle.net/10362/158663
dc.identifier.urlhttps://www.scopus.com/pages/publications/85167420000
dc.language.isoeng
dc.peerreviewedyes
dc.subjectantimony
dc.subjectarsenic
dc.subjectarsenite oxidase
dc.subjectDFT calculations
dc.subjectenzyme mechanism
dc.subjectmolybdenum enzyme
dc.subjectX-ray crystallography
dc.subjectBiochemistry
dc.subjectMolecular Biology
dc.subjectCell Biology
dc.titleArsenite oxidase in complex with antimonite and arsenite oxyanionsen
dc.title.subtitleInsights into the catalytic mechanismen
dc.typejournal article
degois.publication.issue8
degois.publication.titleJournal of Biological Chemistry
degois.publication.volume299
dspace.entity.typePublication
rcaap.rightsopenAccess

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