Structural and electron paramagnetic resonance (EPR) studies of mononuclear molybdenum enzymes from sulfate-reducing bacteria

Detalhes bibliográficos
Autor(a) principal: Brondino, Carlos D.
Data de Publicação: 2006
Outros Autores: Rivas, Maria G., Romão, Maria J., Moura, José J. G., 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/10362/8705
Resumo: Acc. Chem. Res., 2006, 39 (10), pp 788–796 DOI: 10.1021/ar050104k
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spelling Structural and electron paramagnetic resonance (EPR) studies of mononuclear molybdenum enzymes from sulfate-reducing bacteriaAcc. Chem. Res., 2006, 39 (10), pp 788–796 DOI: 10.1021/ar050104kMolybdenum and tungsten are found in biological systems in a mononuclear form in the active site of a diverse group of enzymes that generally catalyze oxygen-atom-transfer reactions. The metal atom (Mo or W) is coordinated to one or two pyranopterin molecules and to a variable number of ligands such as oxygen (oxo, hydroxo, water, serine, aspartic acid), sulfur (cysteines), and selenium (selenocysteines) atoms. In addition, these proteins contain redox cofactors such as iron-sulfur clusters and heme groups. All of these metal cofactors are along an electron-transfer pathway that mediates the electron exchange between substrate and an external electron acceptor (for oxidative reactions) or donor (for reductive reactions). We describe in this Account a combination of structural and electronic paramagnetic resonance studies that were used to reveal distinct aspects of these enzymes.American Chemical SocietyRUNBrondino, Carlos D.Rivas, Maria G.Romão, Maria J.Moura, José J. G.Moura, Isabel2013-02-06T10:44:39Z20062006-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10362/8705eng0001-4842info: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:RCAAP2024-03-11T03:41:35Zoai:run.unl.pt:10362/8705Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:18:23.319662Repositório 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 Structural and electron paramagnetic resonance (EPR) studies of mononuclear molybdenum enzymes from sulfate-reducing bacteria
title Structural and electron paramagnetic resonance (EPR) studies of mononuclear molybdenum enzymes from sulfate-reducing bacteria
spellingShingle Structural and electron paramagnetic resonance (EPR) studies of mononuclear molybdenum enzymes from sulfate-reducing bacteria
Brondino, Carlos D.
title_short Structural and electron paramagnetic resonance (EPR) studies of mononuclear molybdenum enzymes from sulfate-reducing bacteria
title_full Structural and electron paramagnetic resonance (EPR) studies of mononuclear molybdenum enzymes from sulfate-reducing bacteria
title_fullStr Structural and electron paramagnetic resonance (EPR) studies of mononuclear molybdenum enzymes from sulfate-reducing bacteria
title_full_unstemmed Structural and electron paramagnetic resonance (EPR) studies of mononuclear molybdenum enzymes from sulfate-reducing bacteria
title_sort Structural and electron paramagnetic resonance (EPR) studies of mononuclear molybdenum enzymes from sulfate-reducing bacteria
author Brondino, Carlos D.
author_facet Brondino, Carlos D.
Rivas, Maria G.
Romão, Maria J.
Moura, José J. G.
Moura, Isabel
author_role author
author2 Rivas, Maria G.
Romão, Maria J.
Moura, José J. G.
Moura, Isabel
author2_role author
author
author
author
dc.contributor.none.fl_str_mv RUN
dc.contributor.author.fl_str_mv Brondino, Carlos D.
Rivas, Maria G.
Romão, Maria J.
Moura, José J. G.
Moura, Isabel
description Acc. Chem. Res., 2006, 39 (10), pp 788–796 DOI: 10.1021/ar050104k
publishDate 2006
dc.date.none.fl_str_mv 2006
2006-01-01T00:00:00Z
2013-02-06T10:44:39Z
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dc.identifier.uri.fl_str_mv http://hdl.handle.net/10362/8705
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dc.publisher.none.fl_str_mv American Chemical Society
publisher.none.fl_str_mv American Chemical Society
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