Proton-coupled electron transfer mechanisms of the copper centres of nitrous oxide reductase from Marinobacter hydrocarbonoclasticus – An electrochemical study

Detalhes bibliográficos
Autor(a) principal: Carreira, Cíntia
Data de Publicação: 2020
Outros Autores: dos Santos, Margarida M. C., Pauleta, Sofia R., Moura, Isabel
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10362/106731
Resumo: PTDC/BBB-BQB/0129/2014, FCT/MCTES, UID/Multi/04378/2019, UID/QUI/50006/2019, Centro de Quimica Estrutural multiannual funding 2020-2023, UID/QUI/00100/2019.
id RCAP_6cdbec9bcd6ec35cff385764a285d81c
oai_identifier_str oai:run.unl.pt:10362/106731
network_acronym_str RCAP
network_name_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository_id_str 7160
spelling Proton-coupled electron transfer mechanisms of the copper centres of nitrous oxide reductase from Marinobacter hydrocarbonoclasticus – An electrochemical studyCuA centreCuZ centreDirect electrochemistryNitrous oxide reductasePotentiometryProton-coupled electron transferBiophysicsPhysical and Theoretical ChemistryElectrochemistryPTDC/BBB-BQB/0129/2014, FCT/MCTES, UID/Multi/04378/2019, UID/QUI/50006/2019, Centro de Quimica Estrutural multiannual funding 2020-2023, UID/QUI/00100/2019.Reduction of N2O to N2 is catalysed by nitrous oxide reductase in the last step of the denitrification pathway. This multicopper enzyme has an electron transferring centre, CuA, and a tetranuclear copper-sulfide catalytic centre, “CuZ”, which exists as CuZ*(4Cu1S) or CuZ(4Cu2S). The redox behaviour of these metal centres in Marinobacter hydrocarbonoclasticus nitrous oxide reductase was investigated by potentiometry and for the first time by direct electrochemistry. The reduction potential of CuA and CuZ(4Cu2S) was estimated by potentiometry to be +275 ± 5 mV and +65 ± 5 mV vs SHE, respectively, at pH 7.6. A proton-coupled electron transfer mechanism governs CuZ(4Cu2S) reduction potential, due to the protonation/deprotonation of Lys397 with a pKox of 6.0 ± 0.1 and a pKred of 9.2 ± 0.1. The reduction potential of CuA, in enzyme samples with CuZ*(4Cu1S), is controlled by protonation of the coordinating histidine residues in a two-proton coupled electron transfer process. In the cyclic voltammograms, two redox pairs were identified corresponding to CuA and CuZ(4Cu2S), with no additional signals being detected that could be attributed to CuZ*(4Cu1S). However, an enhanced cathodic signal for the activated enzyme was observed under turnover conditions, which is explained by the binding of nitrous oxide to CuZ0(4Cu1S), an intermediate species in the catalytic cycle.LAQV@REQUIMTEUCIBIO - Applied Molecular Biosciences UnitDQ - Departamento de QuímicaRUNCarreira, Cíntiados Santos, Margarida M. C.Pauleta, Sofia R.Moura, Isabel2022-03-08T01:31:21Z2020-06-012020-06-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10362/106731eng1567-5394PURE: 17303556https://doi.org/10.1016/j.bioelechem.2020.107483info: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:RCAAP2024-03-11T04:51:33Zoai:run.unl.pt:10362/106731Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:40:46.252773Repositório 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 Proton-coupled electron transfer mechanisms of the copper centres of nitrous oxide reductase from Marinobacter hydrocarbonoclasticus – An electrochemical study
title Proton-coupled electron transfer mechanisms of the copper centres of nitrous oxide reductase from Marinobacter hydrocarbonoclasticus – An electrochemical study
spellingShingle Proton-coupled electron transfer mechanisms of the copper centres of nitrous oxide reductase from Marinobacter hydrocarbonoclasticus – An electrochemical study
Carreira, Cíntia
CuA centre
CuZ centre
Direct electrochemistry
Nitrous oxide reductase
Potentiometry
Proton-coupled electron transfer
Biophysics
Physical and Theoretical Chemistry
Electrochemistry
title_short Proton-coupled electron transfer mechanisms of the copper centres of nitrous oxide reductase from Marinobacter hydrocarbonoclasticus – An electrochemical study
title_full Proton-coupled electron transfer mechanisms of the copper centres of nitrous oxide reductase from Marinobacter hydrocarbonoclasticus – An electrochemical study
title_fullStr Proton-coupled electron transfer mechanisms of the copper centres of nitrous oxide reductase from Marinobacter hydrocarbonoclasticus – An electrochemical study
title_full_unstemmed Proton-coupled electron transfer mechanisms of the copper centres of nitrous oxide reductase from Marinobacter hydrocarbonoclasticus – An electrochemical study
title_sort Proton-coupled electron transfer mechanisms of the copper centres of nitrous oxide reductase from Marinobacter hydrocarbonoclasticus – An electrochemical study
author Carreira, Cíntia
author_facet Carreira, Cíntia
dos Santos, Margarida M. C.
Pauleta, Sofia R.
Moura, Isabel
author_role author
author2 dos Santos, Margarida M. C.
Pauleta, Sofia R.
Moura, Isabel
author2_role author
author
author
dc.contributor.none.fl_str_mv LAQV@REQUIMTE
UCIBIO - Applied Molecular Biosciences Unit
DQ - Departamento de Química
RUN
dc.contributor.author.fl_str_mv Carreira, Cíntia
dos Santos, Margarida M. C.
Pauleta, Sofia R.
Moura, Isabel
dc.subject.por.fl_str_mv CuA centre
CuZ centre
Direct electrochemistry
Nitrous oxide reductase
Potentiometry
Proton-coupled electron transfer
Biophysics
Physical and Theoretical Chemistry
Electrochemistry
topic CuA centre
CuZ centre
Direct electrochemistry
Nitrous oxide reductase
Potentiometry
Proton-coupled electron transfer
Biophysics
Physical and Theoretical Chemistry
Electrochemistry
description PTDC/BBB-BQB/0129/2014, FCT/MCTES, UID/Multi/04378/2019, UID/QUI/50006/2019, Centro de Quimica Estrutural multiannual funding 2020-2023, UID/QUI/00100/2019.
publishDate 2020
dc.date.none.fl_str_mv 2020-06-01
2020-06-01T00:00:00Z
2022-03-08T01:31:21Z
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/10362/106731
url http://hdl.handle.net/10362/106731
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 1567-5394
PURE: 17303556
https://doi.org/10.1016/j.bioelechem.2020.107483
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
institution RCAAP
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
repository.mail.fl_str_mv
_version_ 1799138021598035968

Registros relacionados