Arsenite oxidase in complex with antimonite and arsenite oxyanions

Detalhes bibliográficos
Autor(a) principal: Engrola, Filipa
Data de Publicação: 2023
Outros Autores: Correia, Márcia A.S., Watson, Cameron, Romão, Carlos C., Veiros, Luis F., Romão, Maria João, Santos-Silva, Teresa, Santini, Joanne M.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10362/158663
Resumo: Funding 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
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spelling Arsenite oxidase in complex with antimonite and arsenite oxyanionsInsights into the catalytic mechanismantimonyarsenicarsenite oxidaseDFT calculationsenzyme mechanismmolybdenum enzymeX-ray crystallographyBiochemistryMolecular BiologyCell BiologyFunding 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 AuthorsArsenic 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.UCIBIO - Applied Molecular Biosciences UnitInstituto de Tecnologia Química e Biológica António Xavier (ITQB)RUNEngrola, FilipaCorreia, Márcia A.S.Watson, CameronRomão, Carlos C.Veiros, Luis F.Romão, Maria JoãoSantos-Silva, TeresaSantini, Joanne M.2023-10-03T22:19:55Z2023-082023-08-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10362/158663eng0021-9258PURE: 72982040https://doi.org/10.1016/j.jbc.2023.105036info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-03-11T05:41:13Zoai:run.unl.pt:10362/158663Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:57:15.782812Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Arsenite oxidase in complex with antimonite and arsenite oxyanions
Insights into the catalytic mechanism
title Arsenite oxidase in complex with antimonite and arsenite oxyanions
spellingShingle Arsenite oxidase in complex with antimonite and arsenite oxyanions
Engrola, Filipa
antimony
arsenic
arsenite oxidase
DFT calculations
enzyme mechanism
molybdenum enzyme
X-ray crystallography
Biochemistry
Molecular Biology
Cell Biology
title_short Arsenite oxidase in complex with antimonite and arsenite oxyanions
title_full Arsenite oxidase in complex with antimonite and arsenite oxyanions
title_fullStr Arsenite oxidase in complex with antimonite and arsenite oxyanions
title_full_unstemmed Arsenite oxidase in complex with antimonite and arsenite oxyanions
title_sort Arsenite oxidase in complex with antimonite and arsenite oxyanions
author Engrola, Filipa
author_facet Engrola, Filipa
Correia, Márcia A.S.
Watson, Cameron
Romão, Carlos C.
Veiros, Luis F.
Romão, Maria João
Santos-Silva, Teresa
Santini, Joanne M.
author_role author
author2 Correia, Márcia A.S.
Watson, Cameron
Romão, Carlos C.
Veiros, Luis F.
Romão, Maria João
Santos-Silva, Teresa
Santini, Joanne M.
author2_role author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv UCIBIO - Applied Molecular Biosciences Unit
Instituto de Tecnologia Química e Biológica António Xavier (ITQB)
RUN
dc.contributor.author.fl_str_mv Engrola, Filipa
Correia, Márcia A.S.
Watson, Cameron
Romão, Carlos C.
Veiros, Luis F.
Romão, Maria João
Santos-Silva, Teresa
Santini, Joanne M.
dc.subject.por.fl_str_mv antimony
arsenic
arsenite oxidase
DFT calculations
enzyme mechanism
molybdenum enzyme
X-ray crystallography
Biochemistry
Molecular Biology
Cell Biology
topic antimony
arsenic
arsenite oxidase
DFT calculations
enzyme mechanism
molybdenum enzyme
X-ray crystallography
Biochemistry
Molecular Biology
Cell Biology
description Funding 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
publishDate 2023
dc.date.none.fl_str_mv 2023-10-03T22:19:55Z
2023-08
2023-08-01T00:00:00Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10362/158663
url http://hdl.handle.net/10362/158663
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 0021-9258
PURE: 72982040
https://doi.org/10.1016/j.jbc.2023.105036
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
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reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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