Mössbauer study of the native, reduced and substrate‐reacted Desulfovibrio gigas aldehyde oxido‐reductase
Autor(a) principal: | |
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Data de Publicação: | 1992 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10362/80774 |
Resumo: | NIGMS NIH HHS (GM41482; GM 32187) |
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7160 |
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Mössbauer study of the native, reduced and substrate‐reacted Desulfovibrio gigas aldehyde oxido‐reductaseBiochemistryNIGMS NIH HHS (GM41482; GM 32187)The Desulfovibrio gigas aldehyde oxido‐reductase contains molybdenum and iron‐sulfur clusters. Mössbauer spectroscopy was used to characterize the iron‐sulfur clusters. Spectra of the enzyme in its oxidized, partially reduced and benzaldehyde‐reacted states were recorded at different temperatures and applied magnetic fields. All the iron atoms in D. gigas aldehyde oxido‐reductase are organized as [2Fe‐2S] clusters. In the oxydized enzyme, the clusters are diamagnetic and exhibit a single quadrupole doublet with parameters (ΔEQ= 0.62 ± 0.02 mm/s and δ= 0.27 ± 0.01 mm/s) typical for the [2Fe‐2S]2+ state. Mössbauer spectra of the reduced clusters also show the characteristics of a [2Fe‐2S]1+ cluster and can be explained by a spin‐coupling model proposed for the [2Fe‐2S] cluster where a high‐spin ferrous ion (S= 2) is antiferromagnetically coupled to a high‐spin ferric ion (S= 5/2) to form a S= 1/2 system. Two ferrous sites with different ΔEQ values (3.42 mm/s and 2.93 mm/s at 85 K) are observed for the reduced enzyme, indicating the presence of two types of [2Fe‐2S] clusters in the D. gigas enzyme. Taking this observation together with the re‐evaluated value of iron content (3.5 ± 0.1 Fe/molecule), it is concluded that, similar to other Mo‐hydroxylases, the D. gigas aldehyde oxido‐reductase also contains two spectroscopically distinguishable [2Fe‐2S] clusters.Instituto de Tecnologia Química e Biológica António Xavier (ITQB)RUNBarata, Belarmino A. S.Liang, JinMoura, IsabelLeGall, JeanMoura, José J. G.Hanh Huynh, Boi2019-09-10T22:49:49Z1992-01-011992-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article6application/pdfhttp://hdl.handle.net/10362/80774eng0014-2956PURE: 14639904http://www.scopus.com/inward/record.url?scp=0026610349&partnerID=8YFLogxKhttps://doi.org/10.1111/j.1432-1033.1992.tb16693.xinfo: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:RCAAP2024-03-11T04:35:45Zoai:run.unl.pt:10362/80774Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:35:56.016798Repositório 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 study of the native, reduced and substrate‐reacted Desulfovibrio gigas aldehyde oxido‐reductase |
title |
Mössbauer study of the native, reduced and substrate‐reacted Desulfovibrio gigas aldehyde oxido‐reductase |
spellingShingle |
Mössbauer study of the native, reduced and substrate‐reacted Desulfovibrio gigas aldehyde oxido‐reductase Barata, Belarmino A. S. Biochemistry |
title_short |
Mössbauer study of the native, reduced and substrate‐reacted Desulfovibrio gigas aldehyde oxido‐reductase |
title_full |
Mössbauer study of the native, reduced and substrate‐reacted Desulfovibrio gigas aldehyde oxido‐reductase |
title_fullStr |
Mössbauer study of the native, reduced and substrate‐reacted Desulfovibrio gigas aldehyde oxido‐reductase |
title_full_unstemmed |
Mössbauer study of the native, reduced and substrate‐reacted Desulfovibrio gigas aldehyde oxido‐reductase |
title_sort |
Mössbauer study of the native, reduced and substrate‐reacted Desulfovibrio gigas aldehyde oxido‐reductase |
author |
Barata, Belarmino A. S. |
author_facet |
Barata, Belarmino A. S. Liang, Jin Moura, Isabel LeGall, Jean Moura, José J. G. Hanh Huynh, Boi |
author_role |
author |
author2 |
Liang, Jin Moura, Isabel LeGall, Jean Moura, José J. G. Hanh Huynh, Boi |
author2_role |
author author author author author |
dc.contributor.none.fl_str_mv |
Instituto de Tecnologia Química e Biológica António Xavier (ITQB) RUN |
dc.contributor.author.fl_str_mv |
Barata, Belarmino A. S. Liang, Jin Moura, Isabel LeGall, Jean Moura, José J. G. Hanh Huynh, Boi |
dc.subject.por.fl_str_mv |
Biochemistry |
topic |
Biochemistry |
description |
NIGMS NIH HHS (GM41482; GM 32187) |
publishDate |
1992 |
dc.date.none.fl_str_mv |
1992-01-01 1992-01-01T00:00:00Z 2019-09-10T22:49:49Z |
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/10362/80774 |
url |
http://hdl.handle.net/10362/80774 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
0014-2956 PURE: 14639904 http://www.scopus.com/inward/record.url?scp=0026610349&partnerID=8YFLogxK https://doi.org/10.1111/j.1432-1033.1992.tb16693.x |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
6 application/pdf |
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 |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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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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1799137979653947392 |