The role of nickel and iron-sulfur centers in the bioproduction of hydrogen

Detalhes bibliográficos
Autor(a) principal: Moura, José J. G.
Data de Publicação: 1989
Outros Autores: Teixeira, Miguel, Moura, Isabel
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
DOI: 10.1351/pac198961050915
Texto Completo: https://doi.org/10.1351/pac198961050915
Resumo: This work was supported by Instituto Nacional de Investiga ao Cientifica (INIC), Junta Nacional de Investigação Cientifica e Tecnológica (JNICT) and 8EE-BAP programs to J.J.G.Moura.
id RCAP_793b3b046fc018224ec9e68cf768c908
oai_identifier_str oai:run.unl.pt:10362/80899
network_acronym_str RCAP
network_name_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository_id_str 7160
spelling The role of nickel and iron-sulfur centers in the bioproduction of hydrogenChemistry(all)Chemical Engineering(all)This work was supported by Instituto Nacional de Investiga ao Cientifica (INIC), Junta Nacional de Investigação Cientifica e Tecnológica (JNICT) and 8EE-BAP programs to J.J.G.Moura.Hydrogenases are generally classified as iron-sulfur-containing proteins with four to twelve iron atoms in different cluster arrangements. Through physiological, chemical and spectroscopic studies, nickel has also been found to be a constitutive metal of several hydrogenases and shown to be involved in a redox linked process. The [NiFe] hydrogenases are now the most intensivelly studied nickel enzymes. Here we will focus on the study of [NiFe] hydrogenases isolated from sulfate reducing bacteria (Desulfovibrio (D.) species). D.gigas hydrogenase is used as a model system for the discussion of the spectroscopic features of the metal centers in the native and hydrogen reacted states. A reasonable understanding of the native enzyme metal center constitution has emerged from EPR and Mossbauer (MB) spectroscopic studies, indicating the presence of four non-interacting centers: one nickel (assigned to be in the unusual trivalent state), one [3Fe-4S] center (EPR active) and two [4Fe-4S] clusters (EPR silent). The intermediate redox species generated under H2 were studied in order to detect the redox processes involved and to determine the associated mid-point potentials. The occuring redox transitions (nickel is assumed to cycle between tri and divalent oxidation states) are related to the redox linked activation step required for the full expression of the enzymatic activity. Special emphasis is given to the interpretation of the EPR and MB results obtained in the enzyme active state and the interplay between the metal centers. The existence of a proton and a hydride acceptor sites are postulated in agreement with a heterolytic cleavage step of the hydrogen molecule. The properties of relevant nickel compounds and functional models, are used in order to define the oxidation states involved and the favored coordination of the nickel site. The assemble of the available experimental data is integrated in the enzyme mechanistic framework. Selenium is also an essential constituent of some [NiFe] hydrogenases. Its role on the fine tuning of the catalytical properties and as a proximal nickel ligand is discussed.Instituto de Tecnologia Química e Biológica António Xavier (ITQB)RUNMoura, José J. G.Teixeira, MiguelMoura, Isabel2019-09-11T22:44:29Z1989-01-011989-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article7application/pdfhttps://doi.org/10.1351/pac198961050915eng0033-4545PURE: 14649904http://www.scopus.com/inward/record.url?scp=0001039966&partnerID=8YFLogxKhttps://doi.org/10.1351/pac198961050915info: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:RCAAP2024-05-22T17:40:53Zoai:run.unl.pt:10362/80899Portal AgregadorONGhttps://www.rcaap.pt/oai/openairemluisa.alvim@gmail.comopendoar:71602024-05-22T17:40:53Repositório 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 The role of nickel and iron-sulfur centers in the bioproduction of hydrogen
title The role of nickel and iron-sulfur centers in the bioproduction of hydrogen
spellingShingle The role of nickel and iron-sulfur centers in the bioproduction of hydrogen
The role of nickel and iron-sulfur centers in the bioproduction of hydrogen
Moura, José J. G.
Chemistry(all)
Chemical Engineering(all)
Moura, José J. G.
Chemistry(all)
Chemical Engineering(all)
title_short The role of nickel and iron-sulfur centers in the bioproduction of hydrogen
title_full The role of nickel and iron-sulfur centers in the bioproduction of hydrogen
title_fullStr The role of nickel and iron-sulfur centers in the bioproduction of hydrogen
The role of nickel and iron-sulfur centers in the bioproduction of hydrogen
title_full_unstemmed The role of nickel and iron-sulfur centers in the bioproduction of hydrogen
The role of nickel and iron-sulfur centers in the bioproduction of hydrogen
title_sort The role of nickel and iron-sulfur centers in the bioproduction of hydrogen
author Moura, José J. G.
author_facet Moura, José J. G.
Moura, José J. G.
Teixeira, Miguel
Moura, Isabel
Teixeira, Miguel
Moura, Isabel
author_role author
author2 Teixeira, Miguel
Moura, Isabel
author2_role author
author
dc.contributor.none.fl_str_mv Instituto de Tecnologia Química e Biológica António Xavier (ITQB)
RUN
dc.contributor.author.fl_str_mv Moura, José J. G.
Teixeira, Miguel
Moura, Isabel
dc.subject.por.fl_str_mv Chemistry(all)
Chemical Engineering(all)
topic Chemistry(all)
Chemical Engineering(all)
description This work was supported by Instituto Nacional de Investiga ao Cientifica (INIC), Junta Nacional de Investigação Cientifica e Tecnológica (JNICT) and 8EE-BAP programs to J.J.G.Moura.
publishDate 1989
dc.date.none.fl_str_mv 1989-01-01
1989-01-01T00:00:00Z
2019-09-11T22:44:29Z
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 https://doi.org/10.1351/pac198961050915
url https://doi.org/10.1351/pac198961050915
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 0033-4545
PURE: 14649904
http://www.scopus.com/inward/record.url?scp=0001039966&partnerID=8YFLogxK
https://doi.org/10.1351/pac198961050915
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 7
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
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str 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 mluisa.alvim@gmail.com
_version_ 1822181944149934080
dc.identifier.doi.none.fl_str_mv 10.1351/pac198961050915

Registros relacionados