Benefits of membrane electrodes in the electrochemistry of metalloproteins: mediated catalysis of Paracoccus pantotrophus cytochrome c peroxidase by horse cytochrome c: a case study

Detalhes bibliográficos
Autor(a) principal: Sousa, P. M. Paes de
Data de Publicação: 2008
Outros Autores: Pauleta, Sofia R., Rodrigues, D., Gonçalves, M. L. Simões, Pettigrew, G. W., Moura, Isabel, Moura, José J. G., Santos, Margarida M. Correia dos
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10362/8699
Resumo: J Biol Inorg Chem. 2008 Jun;13(5):779-87. doi: 10.1007/s00775-008-0365-8
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spelling Benefits of membrane electrodes in the electrochemistry of metalloproteins: mediated catalysis of Paracoccus pantotrophus cytochrome c peroxidase by horse cytochrome c: a case studyMembrane electrodeMediated catalysisBacterial cytochrome c peroxidaseHorse cytochrome cJ Biol Inorg Chem. 2008 Jun;13(5):779-87. doi: 10.1007/s00775-008-0365-8A comparative study of direct and mediated electrochemistry of metalloproteins in bulk and membrane-entrapped solutions is presented. This work reports the first electrochemical study of the electron transfer between a bacterial cytochrome c peroxidase and horse heart cytochrome c. The mediated catalysis of the peroxidase was analysed both using the membrane electrode configuration and with all proteins in solution. An apparent Michaelis constant of 66 +/- 4 and 42 +/- 5 microM was determined at pH 7.0 and 0 M NaCl for membrane and bulk solutions, respectively. The data revealed that maximum activity occurs at 50 mM NaCl, pH 7.0, with intermolecular rate constants of (4.4 +/- 0.5) x 10(6) and (1.0 +/- 0.5) x 10(6) M(-1) s(-1) for membrane-entrapped and bulk solutions, respectively. The influence of parameters such as pH or ionic strength on the mediated catalytic activity was analysed using this approach, drawing attention to the fact that careful analysis of the results is needed to ensure that no artefacts are introduced by the use of the membrane configuration and/or promoters, and therefore the dependence truly reflects the influence of these parameters on the (mediated) catalysis. From the pH dependence, a pK of 7.5 was estimated for the mediated enzymatic catalysis.SpringerRUNSousa, P. M. Paes dePauleta, Sofia R.Rodrigues, D.Gonçalves, M. L. SimõesPettigrew, G. W.Moura, IsabelMoura, José J. G.Santos, Margarida M. Correia dos2013-02-05T16:06:16Z20082008-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10362/8699eng0949-8257info: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:RCAAP2024-03-11T03:41:34Zoai:run.unl.pt:10362/8699Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:18:22.984569Repositório 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 Benefits of membrane electrodes in the electrochemistry of metalloproteins: mediated catalysis of Paracoccus pantotrophus cytochrome c peroxidase by horse cytochrome c: a case study
title Benefits of membrane electrodes in the electrochemistry of metalloproteins: mediated catalysis of Paracoccus pantotrophus cytochrome c peroxidase by horse cytochrome c: a case study
spellingShingle Benefits of membrane electrodes in the electrochemistry of metalloproteins: mediated catalysis of Paracoccus pantotrophus cytochrome c peroxidase by horse cytochrome c: a case study
Sousa, P. M. Paes de
Membrane electrode
Mediated catalysis
Bacterial cytochrome c peroxidase
Horse cytochrome c
title_short Benefits of membrane electrodes in the electrochemistry of metalloproteins: mediated catalysis of Paracoccus pantotrophus cytochrome c peroxidase by horse cytochrome c: a case study
title_full Benefits of membrane electrodes in the electrochemistry of metalloproteins: mediated catalysis of Paracoccus pantotrophus cytochrome c peroxidase by horse cytochrome c: a case study
title_fullStr Benefits of membrane electrodes in the electrochemistry of metalloproteins: mediated catalysis of Paracoccus pantotrophus cytochrome c peroxidase by horse cytochrome c: a case study
title_full_unstemmed Benefits of membrane electrodes in the electrochemistry of metalloproteins: mediated catalysis of Paracoccus pantotrophus cytochrome c peroxidase by horse cytochrome c: a case study
title_sort Benefits of membrane electrodes in the electrochemistry of metalloproteins: mediated catalysis of Paracoccus pantotrophus cytochrome c peroxidase by horse cytochrome c: a case study
author Sousa, P. M. Paes de
author_facet Sousa, P. M. Paes de
Pauleta, Sofia R.
Rodrigues, D.
Gonçalves, M. L. Simões
Pettigrew, G. W.
Moura, Isabel
Moura, José J. G.
Santos, Margarida M. Correia dos
author_role author
author2 Pauleta, Sofia R.
Rodrigues, D.
Gonçalves, M. L. Simões
Pettigrew, G. W.
Moura, Isabel
Moura, José J. G.
Santos, Margarida M. Correia dos
author2_role author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv RUN
dc.contributor.author.fl_str_mv Sousa, P. M. Paes de
Pauleta, Sofia R.
Rodrigues, D.
Gonçalves, M. L. Simões
Pettigrew, G. W.
Moura, Isabel
Moura, José J. G.
Santos, Margarida M. Correia dos
dc.subject.por.fl_str_mv Membrane electrode
Mediated catalysis
Bacterial cytochrome c peroxidase
Horse cytochrome c
topic Membrane electrode
Mediated catalysis
Bacterial cytochrome c peroxidase
Horse cytochrome c
description J Biol Inorg Chem. 2008 Jun;13(5):779-87. doi: 10.1007/s00775-008-0365-8
publishDate 2008
dc.date.none.fl_str_mv 2008
2008-01-01T00:00:00Z
2013-02-05T16:06:16Z
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/10362/8699
url http://hdl.handle.net/10362/8699
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 0949-8257
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.publisher.none.fl_str_mv Springer
publisher.none.fl_str_mv Springer
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
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