Voltammetric studies of the catalytic electron‐transfer process between the Desulfovibrio gigas hydrogenase and small proteins isolated from the same genus
Autor(a) principal: | |
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Data de Publicação: | 1993 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | https://doi.org/10.1111/j.1432-1033.1993.tb18329.x |
Resumo: | The kinetics of electron transfer between the Desulfovibrio gigas hydrogenase and several electron‐transfer proteins from Desulfovibrio species were investigated by cyclic voltammetry, square‐wave voltammetry and chronoamperometry. The cytochrome c3 from Desulfovibrio vulgaris (Hil‐denborough), Desulfovibrio desulfuricans (Norway 4), Desulfovibrio desulfuricans (American Type Culture Collection 27774) and D. gigas (NCIB 9332) were used as redox carriers. They differ in their redox potentials and isoelectric point. Depending on the pH, all the reduced forms of these cytochromes were effective in electron exchange with hydrogenase. Other small electron‐transfer proteins such as ferredoxin I, ferredoxin II and rubredoxin from D. gigas were tentatively used as redox carriers. Only ferredoxin II was effective in mediating electron exchange between hydrogenase and the working electrode. The second‐order rate constants k for the reaction between reduced proteins and hydrogenase were calculated based on the theory of the simplest electrocatalytic mechanism [Moreno, C., Costa, C., Moura, I., Le Gall, J., Liu, M. Y., Payne, W. J., van Dijk, C. & Moura, J. J. G. (1993) Eur. J. Biochem. 212, 79–86] and the results obtained by cyclic voltammetry were compared with those obtained by chronoamperometry. Values for k of 105–106 M−1 s−1 (cytochrome c3 as electron carrier) and 104 M−1 s−1 (ferredoxin II as the electron carrier) were determined. The rate‐constant values are discussed in terms of the existence of an electrostatic interaction between the electrode surface and the redox carrier and between the redox carrier and a positively charged part of the enzyme. |
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Voltammetric studies of the catalytic electron‐transfer process between the Desulfovibrio gigas hydrogenase and small proteins isolated from the same genusBiochemistryThe kinetics of electron transfer between the Desulfovibrio gigas hydrogenase and several electron‐transfer proteins from Desulfovibrio species were investigated by cyclic voltammetry, square‐wave voltammetry and chronoamperometry. The cytochrome c3 from Desulfovibrio vulgaris (Hil‐denborough), Desulfovibrio desulfuricans (Norway 4), Desulfovibrio desulfuricans (American Type Culture Collection 27774) and D. gigas (NCIB 9332) were used as redox carriers. They differ in their redox potentials and isoelectric point. Depending on the pH, all the reduced forms of these cytochromes were effective in electron exchange with hydrogenase. Other small electron‐transfer proteins such as ferredoxin I, ferredoxin II and rubredoxin from D. gigas were tentatively used as redox carriers. Only ferredoxin II was effective in mediating electron exchange between hydrogenase and the working electrode. The second‐order rate constants k for the reaction between reduced proteins and hydrogenase were calculated based on the theory of the simplest electrocatalytic mechanism [Moreno, C., Costa, C., Moura, I., Le Gall, J., Liu, M. Y., Payne, W. J., van Dijk, C. & Moura, J. J. G. (1993) Eur. J. Biochem. 212, 79–86] and the results obtained by cyclic voltammetry were compared with those obtained by chronoamperometry. Values for k of 105–106 M−1 s−1 (cytochrome c3 as electron carrier) and 104 M−1 s−1 (ferredoxin II as the electron carrier) were determined. The rate‐constant values are discussed in terms of the existence of an electrostatic interaction between the electrode surface and the redox carrier and between the redox carrier and a positively charged part of the enzyme.DQ - Departamento de QuímicaRUNMoreno, CristinaFranco, RicardoMoura, IsabelLe Gall, JeanMOURA, José J. G.2019-09-10T22:49:42Z1993-01-011993-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article9application/pdfhttps://doi.org/10.1111/j.1432-1033.1993.tb18329.xeng0014-2956PURE: 14637579http://www.scopus.com/inward/record.url?scp=0027372952&partnerID=8YFLogxKhttps://doi.org/10.1111/j.1432-1033.1993.tb18329.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:10362/80771Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:35:55.864905Repositório 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 |
Voltammetric studies of the catalytic electron‐transfer process between the Desulfovibrio gigas hydrogenase and small proteins isolated from the same genus |
title |
Voltammetric studies of the catalytic electron‐transfer process between the Desulfovibrio gigas hydrogenase and small proteins isolated from the same genus |
spellingShingle |
Voltammetric studies of the catalytic electron‐transfer process between the Desulfovibrio gigas hydrogenase and small proteins isolated from the same genus Moreno, Cristina Biochemistry |
title_short |
Voltammetric studies of the catalytic electron‐transfer process between the Desulfovibrio gigas hydrogenase and small proteins isolated from the same genus |
title_full |
Voltammetric studies of the catalytic electron‐transfer process between the Desulfovibrio gigas hydrogenase and small proteins isolated from the same genus |
title_fullStr |
Voltammetric studies of the catalytic electron‐transfer process between the Desulfovibrio gigas hydrogenase and small proteins isolated from the same genus |
title_full_unstemmed |
Voltammetric studies of the catalytic electron‐transfer process between the Desulfovibrio gigas hydrogenase and small proteins isolated from the same genus |
title_sort |
Voltammetric studies of the catalytic electron‐transfer process between the Desulfovibrio gigas hydrogenase and small proteins isolated from the same genus |
author |
Moreno, Cristina |
author_facet |
Moreno, Cristina Franco, Ricardo Moura, Isabel Le Gall, Jean MOURA, José J. G. |
author_role |
author |
author2 |
Franco, Ricardo Moura, Isabel Le Gall, Jean MOURA, José J. G. |
author2_role |
author author author author |
dc.contributor.none.fl_str_mv |
DQ - Departamento de Química RUN |
dc.contributor.author.fl_str_mv |
Moreno, Cristina Franco, Ricardo Moura, Isabel Le Gall, Jean MOURA, José J. G. |
dc.subject.por.fl_str_mv |
Biochemistry |
topic |
Biochemistry |
description |
The kinetics of electron transfer between the Desulfovibrio gigas hydrogenase and several electron‐transfer proteins from Desulfovibrio species were investigated by cyclic voltammetry, square‐wave voltammetry and chronoamperometry. The cytochrome c3 from Desulfovibrio vulgaris (Hil‐denborough), Desulfovibrio desulfuricans (Norway 4), Desulfovibrio desulfuricans (American Type Culture Collection 27774) and D. gigas (NCIB 9332) were used as redox carriers. They differ in their redox potentials and isoelectric point. Depending on the pH, all the reduced forms of these cytochromes were effective in electron exchange with hydrogenase. Other small electron‐transfer proteins such as ferredoxin I, ferredoxin II and rubredoxin from D. gigas were tentatively used as redox carriers. Only ferredoxin II was effective in mediating electron exchange between hydrogenase and the working electrode. The second‐order rate constants k for the reaction between reduced proteins and hydrogenase were calculated based on the theory of the simplest electrocatalytic mechanism [Moreno, C., Costa, C., Moura, I., Le Gall, J., Liu, M. Y., Payne, W. J., van Dijk, C. & Moura, J. J. G. (1993) Eur. J. Biochem. 212, 79–86] and the results obtained by cyclic voltammetry were compared with those obtained by chronoamperometry. Values for k of 105–106 M−1 s−1 (cytochrome c3 as electron carrier) and 104 M−1 s−1 (ferredoxin II as the electron carrier) were determined. The rate‐constant values are discussed in terms of the existence of an electrostatic interaction between the electrode surface and the redox carrier and between the redox carrier and a positively charged part of the enzyme. |
publishDate |
1993 |
dc.date.none.fl_str_mv |
1993-01-01 1993-01-01T00:00:00Z 2019-09-10T22:49:42Z |
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/10.1111/j.1432-1033.1993.tb18329.x |
url |
https://doi.org/10.1111/j.1432-1033.1993.tb18329.x |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
0014-2956 PURE: 14637579 http://www.scopus.com/inward/record.url?scp=0027372952&partnerID=8YFLogxK https://doi.org/10.1111/j.1432-1033.1993.tb18329.x |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
9 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 |
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1799137979649753088 |