Mössbauer characterization of Paracoccus denitrificans cytochrome c peroxidase: Further evidence for redox and calcium binding-induced heme-heme interaction

Detalhes bibliográficos
Autor(a) principal: Prazeres, Susana
Data de Publicação: 1995
Outros Autores: Moura, José J. G., Moura, Isabel, Gilmour, Raymond, Goodhew, Celia F., Pettigrew, Graham W., Ravi, Natarajan, Huynh, Boi Hanh
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: https://doi.org/10.1074/jbc.270.41.24264
Resumo: Wellcome Trust NIGMS NIH HHS (GM 47295)
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spelling Mössbauer characterization of Paracoccus denitrificans cytochrome c peroxidase: Further evidence for redox and calcium binding-induced heme-heme interactionBiochemistryMolecular BiologyCell BiologyWellcome Trust NIGMS NIH HHS (GM 47295)Mössbauer and electron paramagnetic resonance (EPR) spectroscopies were used to characterize the diheme cytochrome c peroxidase from Paracoccus denitrificans (L.M.D. 52.44). The spectra of the oxidized enzyme show two distinct spectral components characteristic of low spin ferric hemes (S = 1/2), revealing different heme environments for the two heme groups. The Paracoccus peroxidase can be non-physiologically reduced by ascorbate. Mössbauer investigation of the ascorbate-reduced peroxidase shows that only one heme (the high potential heme) is reduced and that the reduced heme is diamagnetic (S = 0). The other heme (the low potential heme) remains oxidized, indicating that the enzyme is in a mixed valence, half-reduced state. The EPR spectrum of the half-reduced peroxidase, however, shows two low spin ferric species with gmax = 2.89 (species I) and gmax = 2.78 (species II). This EPR observation, together with the Mössbauer result, suggests that both species are arising from the low potential heme. More interestingly, the spectroscopic properties of these two species are distinct from that of the low potential heme in the oxidized enzyme, providing evidence for heme-heme interaction induced by the reduction of the high potential heme. Addition of calcium ions to the half-reduced enzyme converts species II to species I. Since calcium has been found to promote peroxidase activity, species I may represent the active form of the peroxidatic heme.DQ - Departamento de QuímicaRUNPrazeres, SusanaMoura, José J. G.Moura, IsabelGilmour, RaymondGoodhew, Celia F.Pettigrew, Graham W.Ravi, NatarajanHuynh, Boi Hanh2019-09-10T22:49:29Z1995-10-131995-10-13T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article6application/pdfhttps://doi.org/10.1074/jbc.270.41.24264eng0021-9258PURE: 14632550http://www.scopus.com/inward/record.url?scp=0028972074&partnerID=8YFLogxKhttps://doi.org/10.1074/jbc.270.41.24264info: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:RCAAP2024-03-11T04:35:44Zoai:run.unl.pt:10362/80767Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:35:55.660965Repositório 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 Mössbauer characterization of Paracoccus denitrificans cytochrome c peroxidase: Further evidence for redox and calcium binding-induced heme-heme interaction
title Mössbauer characterization of Paracoccus denitrificans cytochrome c peroxidase: Further evidence for redox and calcium binding-induced heme-heme interaction
spellingShingle Mössbauer characterization of Paracoccus denitrificans cytochrome c peroxidase: Further evidence for redox and calcium binding-induced heme-heme interaction
Prazeres, Susana
Biochemistry
Molecular Biology
Cell Biology
title_short Mössbauer characterization of Paracoccus denitrificans cytochrome c peroxidase: Further evidence for redox and calcium binding-induced heme-heme interaction
title_full Mössbauer characterization of Paracoccus denitrificans cytochrome c peroxidase: Further evidence for redox and calcium binding-induced heme-heme interaction
title_fullStr Mössbauer characterization of Paracoccus denitrificans cytochrome c peroxidase: Further evidence for redox and calcium binding-induced heme-heme interaction
title_full_unstemmed Mössbauer characterization of Paracoccus denitrificans cytochrome c peroxidase: Further evidence for redox and calcium binding-induced heme-heme interaction
title_sort Mössbauer characterization of Paracoccus denitrificans cytochrome c peroxidase: Further evidence for redox and calcium binding-induced heme-heme interaction
author Prazeres, Susana
author_facet Prazeres, Susana
Moura, José J. G.
Moura, Isabel
Gilmour, Raymond
Goodhew, Celia F.
Pettigrew, Graham W.
Ravi, Natarajan
Huynh, Boi Hanh
author_role author
author2 Moura, José J. G.
Moura, Isabel
Gilmour, Raymond
Goodhew, Celia F.
Pettigrew, Graham W.
Ravi, Natarajan
Huynh, Boi Hanh
author2_role author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv DQ - Departamento de Química
RUN
dc.contributor.author.fl_str_mv Prazeres, Susana
Moura, José J. G.
Moura, Isabel
Gilmour, Raymond
Goodhew, Celia F.
Pettigrew, Graham W.
Ravi, Natarajan
Huynh, Boi Hanh
dc.subject.por.fl_str_mv Biochemistry
Molecular Biology
Cell Biology
topic Biochemistry
Molecular Biology
Cell Biology
description Wellcome Trust NIGMS NIH HHS (GM 47295)
publishDate 1995
dc.date.none.fl_str_mv 1995-10-13
1995-10-13T00:00:00Z
2019-09-10T22:49:29Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
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status_str publishedVersion
dc.identifier.uri.fl_str_mv https://doi.org/10.1074/jbc.270.41.24264
url https://doi.org/10.1074/jbc.270.41.24264
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 0021-9258
PURE: 14632550
http://www.scopus.com/inward/record.url?scp=0028972074&partnerID=8YFLogxK
https://doi.org/10.1074/jbc.270.41.24264
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