Electrochemical studies of the hexaheme nitrite reductase from Desulfovibrio desulfuricans ATCC 27774
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.tb17635.x |
Resumo: | The electron‐transfer kinetics between three different mediators and the hexahemic enzyme nitrite reductase isolated from Desulfovibrio desulfuricans (ATCC 27774) were investigated by cyclic voltammetry and by chronoamperometry. The mediators, methyl viologen, Desulfovibrio vulgaris (Hildenborough) cytochrome c3 and D. desulfuricans (ATCC 27774) cytochrome c3 differ in structure, redox potential and charge. The reduced form of each mediator exchanged electrons with nitrite reductase. Second‐order rate constants, k, were calculated on the basis of the theory for a simple catalytic mechanism and the results, obtained by cyclic voltammetry, were compared with those obtained by chronoamperometry. Values for k are in the range 106–108 M−1 s−1 and increase in the direction D. desulfuricans cytochrome c3→D. vulgaris cytochrome c3→ methyl viologen. An explanation is advanced on the basis of electrostatic interactions and relative orientation between the partners involved. Chronoamperometry (computer controlled) offers advantages over cyclic voltammetry in the determination of homogeneous rate constants (faster, more accurate and better reproducibility). Direct, unmediated electrochemical responses of the hexaheme nitrite reductase were also reported. |
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Electrochemical studies of the hexaheme nitrite reductase from Desulfovibrio desulfuricans ATCC 27774BiochemistryThe electron‐transfer kinetics between three different mediators and the hexahemic enzyme nitrite reductase isolated from Desulfovibrio desulfuricans (ATCC 27774) were investigated by cyclic voltammetry and by chronoamperometry. The mediators, methyl viologen, Desulfovibrio vulgaris (Hildenborough) cytochrome c3 and D. desulfuricans (ATCC 27774) cytochrome c3 differ in structure, redox potential and charge. The reduced form of each mediator exchanged electrons with nitrite reductase. Second‐order rate constants, k, were calculated on the basis of the theory for a simple catalytic mechanism and the results, obtained by cyclic voltammetry, were compared with those obtained by chronoamperometry. Values for k are in the range 106–108 M−1 s−1 and increase in the direction D. desulfuricans cytochrome c3→D. vulgaris cytochrome c3→ methyl viologen. An explanation is advanced on the basis of electrostatic interactions and relative orientation between the partners involved. Chronoamperometry (computer controlled) offers advantages over cyclic voltammetry in the determination of homogeneous rate constants (faster, more accurate and better reproducibility). Direct, unmediated electrochemical responses of the hexaheme nitrite reductase were also reported.DQ - Departamento de QuímicaInstituto de Tecnologia Química e Biológica António Xavier (ITQB)RUNMoreno, CristinaCosta, CristinaMOURA, IsabelLe Gall, JeanLiu, Ming Y.Payne, William J.van Dijk, CeesMoura, José J. G.2019-09-10T22:49:44Z1993-01-011993-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article8application/pdfhttps://doi.org/10.1111/j.1432-1033.1993.tb17635.xeng0014-2956PURE: 14638751http://www.scopus.com/inward/record.url?scp=0027500304&partnerID=8YFLogxKhttps://doi.org/10.1111/j.1432-1033.1993.tb17635.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:10362/80772Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:35:55.912465Repositório 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 |
Electrochemical studies of the hexaheme nitrite reductase from Desulfovibrio desulfuricans ATCC 27774 |
title |
Electrochemical studies of the hexaheme nitrite reductase from Desulfovibrio desulfuricans ATCC 27774 |
spellingShingle |
Electrochemical studies of the hexaheme nitrite reductase from Desulfovibrio desulfuricans ATCC 27774 Moreno, Cristina Biochemistry |
title_short |
Electrochemical studies of the hexaheme nitrite reductase from Desulfovibrio desulfuricans ATCC 27774 |
title_full |
Electrochemical studies of the hexaheme nitrite reductase from Desulfovibrio desulfuricans ATCC 27774 |
title_fullStr |
Electrochemical studies of the hexaheme nitrite reductase from Desulfovibrio desulfuricans ATCC 27774 |
title_full_unstemmed |
Electrochemical studies of the hexaheme nitrite reductase from Desulfovibrio desulfuricans ATCC 27774 |
title_sort |
Electrochemical studies of the hexaheme nitrite reductase from Desulfovibrio desulfuricans ATCC 27774 |
author |
Moreno, Cristina |
author_facet |
Moreno, Cristina Costa, Cristina MOURA, Isabel Le Gall, Jean Liu, Ming Y. Payne, William J. van Dijk, Cees Moura, José J. G. |
author_role |
author |
author2 |
Costa, Cristina MOURA, Isabel Le Gall, Jean Liu, Ming Y. Payne, William J. van Dijk, Cees Moura, José J. G. |
author2_role |
author author author author author author author |
dc.contributor.none.fl_str_mv |
DQ - Departamento de Química Instituto de Tecnologia Química e Biológica António Xavier (ITQB) RUN |
dc.contributor.author.fl_str_mv |
Moreno, Cristina Costa, Cristina MOURA, Isabel Le Gall, Jean Liu, Ming Y. Payne, William J. van Dijk, Cees Moura, José J. G. |
dc.subject.por.fl_str_mv |
Biochemistry |
topic |
Biochemistry |
description |
The electron‐transfer kinetics between three different mediators and the hexahemic enzyme nitrite reductase isolated from Desulfovibrio desulfuricans (ATCC 27774) were investigated by cyclic voltammetry and by chronoamperometry. The mediators, methyl viologen, Desulfovibrio vulgaris (Hildenborough) cytochrome c3 and D. desulfuricans (ATCC 27774) cytochrome c3 differ in structure, redox potential and charge. The reduced form of each mediator exchanged electrons with nitrite reductase. Second‐order rate constants, k, were calculated on the basis of the theory for a simple catalytic mechanism and the results, obtained by cyclic voltammetry, were compared with those obtained by chronoamperometry. Values for k are in the range 106–108 M−1 s−1 and increase in the direction D. desulfuricans cytochrome c3→D. vulgaris cytochrome c3→ methyl viologen. An explanation is advanced on the basis of electrostatic interactions and relative orientation between the partners involved. Chronoamperometry (computer controlled) offers advantages over cyclic voltammetry in the determination of homogeneous rate constants (faster, more accurate and better reproducibility). Direct, unmediated electrochemical responses of the hexaheme nitrite reductase were also reported. |
publishDate |
1993 |
dc.date.none.fl_str_mv |
1993-01-01 1993-01-01T00:00:00Z 2019-09-10T22:49:44Z |
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.tb17635.x |
url |
https://doi.org/10.1111/j.1432-1033.1993.tb17635.x |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
0014-2956 PURE: 14638751 http://www.scopus.com/inward/record.url?scp=0027500304&partnerID=8YFLogxK https://doi.org/10.1111/j.1432-1033.1993.tb17635.x |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
8 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 |
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 |
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1799137979650801664 |