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

Bibliographic Details
Main Author: Carreira, Cíntia
Publication Date: 2020
Other Authors: dos Santos, Margarida M. C., Pauleta, Sofia R., Moura, Isabel
Format: Article
Language: eng
Source: Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
Download full: http://hdl.handle.net/10362/106731
Summary: 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.
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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:Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)instname:FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiainstacron:RCAAP2024-05-22T17:48:30Zoai:run.unl.pt:10362/106731Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireinfo@rcaap.ptopendoar:https://opendoar.ac.uk/repository/71602025-05-28T17:19:42.193672Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) - FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiafalse
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:Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
instname:FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologia
instacron:RCAAP
instname_str FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologia
instacron_str RCAAP
institution RCAAP
reponame_str Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
collection Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
repository.name.fl_str_mv Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) - FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologia
repository.mail.fl_str_mv info@rcaap.pt
_version_ 1833596615325122560

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