Correlating EPR and X-ray structural analysis of arsenite-inhibited forms of aldehyde oxidoreductase

Detalhes bibliográficos
Autor(a) principal: Thapper, Anders
Data de Publicação: 2006
Outros Autores: Boer, D. R., Brondino, Carlos D., Moura, José J. G., Romão, Maria J.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10362/8704
Resumo: J Biol Inorg Chem (2007) 12:353–366 DOI 10.1007/s00775-006-0191-9
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spelling Correlating EPR and X-ray structural analysis of arsenite-inhibited forms of aldehyde oxidoreductaseMolybdenum-containing enzymesAldehyde oxidoreductaseXanthine oxidase familyElectron paramagnetic resonanceX-rayJ Biol Inorg Chem (2007) 12:353–366 DOI 10.1007/s00775-006-0191-9Two arsenite-inhibited forms of each of the aldehyde oxidoreductases from Desulfovibrio gigas and Desulfovibrio desulfuricans have been studied by X-ray crystallography and electron paramagnetic resonance (EPR) spectroscopy. The molybdenum site of these enzymes shows a distorted square-pyramidal geometry in which two ligands, a hydroxyl/water molecule (the catalytic labile site) and a sulfido ligand, have been shown to be essential for catalysis. Arsenite addition to active as-prepared enzyme or to a reduced desulfo form yields two different species called A and B, respectively, which show different Mo(V) EPR signals. Both EPR signals show strong hyperfine and quadrupolar couplings with an arsenic nucleus, which suggests that arsenic interacts with molybdenum through an equatorial ligand. X-ray data of single crystals prepared from EPR-active samples show in both inhibited forms that the arsenic atom interacts with the molybdenum ion through an oxygen atom at the catalytic labile site and that the sulfido ligand is no longer present. EPR and X-ray data indicate that the main difference between both species is an equatorial ligand to molybdenum which was determined to be an oxo ligand in species A and a hydroxyl/water ligand in species B. The conclusion that the sulfido ligand is not essential to determine the EPR properties in both Mo-As complexes is achieved through EPR measurements on a substantial number of randomly oriented chemically reduced crystals immediately followed by X-ray studies on one of those crystals. EPR saturation studies show that the electron transfer pathway, which is essential for catalysis, is not modified upon inhibition.SpringerRUNThapper, AndersBoer, D. R.Brondino, Carlos D.Moura, José J. G.Romão, Maria J.2013-02-06T10:34:05Z20062006-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10362/8704eng0949-8257info: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:RCAAP2024-03-11T03:41:35Zoai:run.unl.pt:10362/8704Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:18:23.276384Repositório 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 Correlating EPR and X-ray structural analysis of arsenite-inhibited forms of aldehyde oxidoreductase
title Correlating EPR and X-ray structural analysis of arsenite-inhibited forms of aldehyde oxidoreductase
spellingShingle Correlating EPR and X-ray structural analysis of arsenite-inhibited forms of aldehyde oxidoreductase
Thapper, Anders
Molybdenum-containing enzymes
Aldehyde oxidoreductase
Xanthine oxidase family
Electron paramagnetic resonance
X-ray
title_short Correlating EPR and X-ray structural analysis of arsenite-inhibited forms of aldehyde oxidoreductase
title_full Correlating EPR and X-ray structural analysis of arsenite-inhibited forms of aldehyde oxidoreductase
title_fullStr Correlating EPR and X-ray structural analysis of arsenite-inhibited forms of aldehyde oxidoreductase
title_full_unstemmed Correlating EPR and X-ray structural analysis of arsenite-inhibited forms of aldehyde oxidoreductase
title_sort Correlating EPR and X-ray structural analysis of arsenite-inhibited forms of aldehyde oxidoreductase
author Thapper, Anders
author_facet Thapper, Anders
Boer, D. R.
Brondino, Carlos D.
Moura, José J. G.
Romão, Maria J.
author_role author
author2 Boer, D. R.
Brondino, Carlos D.
Moura, José J. G.
Romão, Maria J.
author2_role author
author
author
author
dc.contributor.none.fl_str_mv RUN
dc.contributor.author.fl_str_mv Thapper, Anders
Boer, D. R.
Brondino, Carlos D.
Moura, José J. G.
Romão, Maria J.
dc.subject.por.fl_str_mv Molybdenum-containing enzymes
Aldehyde oxidoreductase
Xanthine oxidase family
Electron paramagnetic resonance
X-ray
topic Molybdenum-containing enzymes
Aldehyde oxidoreductase
Xanthine oxidase family
Electron paramagnetic resonance
X-ray
description J Biol Inorg Chem (2007) 12:353–366 DOI 10.1007/s00775-006-0191-9
publishDate 2006
dc.date.none.fl_str_mv 2006
2006-01-01T00:00:00Z
2013-02-06T10:34:05Z
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/10362/8704
url http://hdl.handle.net/10362/8704
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
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reponame_str 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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