A copper protein and a cytochrome bind at the same site on bacterial cytochrome c peroxidase

Detalhes bibliográficos
Autor(a) principal: Pauleta, Sofia R.
Data de Publicação: 2004
Outros Autores: Cooper, Alan, Nutley, Margaret, Errington, Neil, Goodhew, Celia F., Moura, Isabel, Moura, José J. G.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10362/8711
Resumo: Biochemistry, 2004, 43 (46), pp 14566–14576 DOI: 10.1021/bi0485833
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spelling A copper protein and a cytochrome bind at the same site on bacterial cytochrome c peroxidaseBiochemistry, 2004, 43 (46), pp 14566–14576 DOI: 10.1021/bi0485833Pseudoazurin binds at a single site on cytochrome c peroxidase from Paracoccus pantotrophus with a K(d) of 16.4 microM at 25 degrees C, pH 6.0, in an endothermic reaction that is driven by a large entropy change. Sedimentation velocity experiments confirmed the presence of a single site, although results at higher pseudoazurin concentrations are complicated by the dimerization of the protein. Microcalorimetry, ultracentrifugation, and (1)H NMR spectroscopy studies in which cytochrome c550, pseudoazurin, and cytochrome c peroxidase were all present could be modeled using a competitive binding algorithm. Molecular docking simulation of the binding of pseudoazurin to the peroxidase in combination with the chemical shift perturbation pattern for pseudoazurin in the presence of the peroxidase revealed a group of solutions that were situated close to the electron-transferring heme with Cu-Fe distances of about 14 A. This is consistent with the results of (1)H NMR spectroscopy, which showed that pseudoazurin binds closely enough to the electron-transferring heme of the peroxidase to perturb its set of heme methyl resonances. We conclude that cytochrome c550 and pseudoazurin bind at the same site on the cytochrome c peroxidase and that the pair of electrons required to restore the enzyme to its active state after turnover are delivered one-by-one to the electron-transferring heme.American Chemical SocietyRUNPauleta, Sofia R.Cooper, AlanNutley, MargaretErrington, NeilGoodhew, Celia F.Moura, IsabelMoura, José J. G.2013-02-06T11:55:21Z20042004-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10362/8711eng0006-2960info: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:RCAAP2024-03-11T03:41:36Zoai:run.unl.pt:10362/8711Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:18:23.558901Repositório 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 A copper protein and a cytochrome bind at the same site on bacterial cytochrome c peroxidase
title A copper protein and a cytochrome bind at the same site on bacterial cytochrome c peroxidase
spellingShingle A copper protein and a cytochrome bind at the same site on bacterial cytochrome c peroxidase
Pauleta, Sofia R.
title_short A copper protein and a cytochrome bind at the same site on bacterial cytochrome c peroxidase
title_full A copper protein and a cytochrome bind at the same site on bacterial cytochrome c peroxidase
title_fullStr A copper protein and a cytochrome bind at the same site on bacterial cytochrome c peroxidase
title_full_unstemmed A copper protein and a cytochrome bind at the same site on bacterial cytochrome c peroxidase
title_sort A copper protein and a cytochrome bind at the same site on bacterial cytochrome c peroxidase
author Pauleta, Sofia R.
author_facet Pauleta, Sofia R.
Cooper, Alan
Nutley, Margaret
Errington, Neil
Goodhew, Celia F.
Moura, Isabel
Moura, José J. G.
author_role author
author2 Cooper, Alan
Nutley, Margaret
Errington, Neil
Goodhew, Celia F.
Moura, Isabel
Moura, José J. G.
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv RUN
dc.contributor.author.fl_str_mv Pauleta, Sofia R.
Cooper, Alan
Nutley, Margaret
Errington, Neil
Goodhew, Celia F.
Moura, Isabel
Moura, José J. G.
description Biochemistry, 2004, 43 (46), pp 14566–14576 DOI: 10.1021/bi0485833
publishDate 2004
dc.date.none.fl_str_mv 2004
2004-01-01T00:00:00Z
2013-02-06T11:55:21Z
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/10362/8711
url http://hdl.handle.net/10362/8711
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 0006-2960
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 American Chemical Society
publisher.none.fl_str_mv American Chemical Society
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
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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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