Electrochemical Kinetics Support a Second Coordination Sphere Mechanism in Metal‐Based Formate Dehydrogenase
Autor(a) principal: | |
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Data de Publicação: | 2023 |
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/10362/158534 |
Resumo: | Metal-based formate dehydrogenases are molybdenum or tungsten-dependent enzymes that catalyze the interconversion between formate and CO2. According to the current consensus, the metal ion of the catalytic center in its active form is coordinated by 6 S (or 5 S and 1 Se) atoms, leaving no free coordination sites to which formate could bind to the metal. Some authors have proposed that one of the active site ligands decoordinates during turnover to allow formate binding. Another proposal is that the oxidation of formate takes place in the second coordination sphere of the metal. Here, we have used electrochemical steady-state kinetics to elucidate the order of the steps in the catalytic cycle of two formate dehydrogenases. Our results strongly support the “second coordination sphere” hypothesis. |
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Electrochemical Kinetics Support a Second Coordination Sphere Mechanism in Metal‐Based Formate DehydrogenaseMetal-based formate dehydrogenases are molybdenum or tungsten-dependent enzymes that catalyze the interconversion between formate and CO2. According to the current consensus, the metal ion of the catalytic center in its active form is coordinated by 6 S (or 5 S and 1 Se) atoms, leaving no free coordination sites to which formate could bind to the metal. Some authors have proposed that one of the active site ligands decoordinates during turnover to allow formate binding. Another proposal is that the oxidation of formate takes place in the second coordination sphere of the metal. Here, we have used electrochemical steady-state kinetics to elucidate the order of the steps in the catalytic cycle of two formate dehydrogenases. Our results strongly support the “second coordination sphere” hypothesis.Instituto de Tecnologia Química e Biológica António Xavier (ITQB)RUNMeneghello, MartaUzel, AlexandreBroc, MarianneManuel, Rita R.Magalon, AxelLéger, ChristophePereira, Inês a. c.Walburger, AnneFourmond, Vincent2023-09-30T22:20:29Z2023-02-012023-02-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10362/158534eng1433-7851PURE: 72579828https://doi.org/10.1002/anie.202212224info: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:RCAAP2024-03-11T05:41:01Zoai:run.unl.pt:10362/158534Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:57:11.755358Repositório 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 Kinetics Support a Second Coordination Sphere Mechanism in Metal‐Based Formate Dehydrogenase |
title |
Electrochemical Kinetics Support a Second Coordination Sphere Mechanism in Metal‐Based Formate Dehydrogenase |
spellingShingle |
Electrochemical Kinetics Support a Second Coordination Sphere Mechanism in Metal‐Based Formate Dehydrogenase Meneghello, Marta |
title_short |
Electrochemical Kinetics Support a Second Coordination Sphere Mechanism in Metal‐Based Formate Dehydrogenase |
title_full |
Electrochemical Kinetics Support a Second Coordination Sphere Mechanism in Metal‐Based Formate Dehydrogenase |
title_fullStr |
Electrochemical Kinetics Support a Second Coordination Sphere Mechanism in Metal‐Based Formate Dehydrogenase |
title_full_unstemmed |
Electrochemical Kinetics Support a Second Coordination Sphere Mechanism in Metal‐Based Formate Dehydrogenase |
title_sort |
Electrochemical Kinetics Support a Second Coordination Sphere Mechanism in Metal‐Based Formate Dehydrogenase |
author |
Meneghello, Marta |
author_facet |
Meneghello, Marta Uzel, Alexandre Broc, Marianne Manuel, Rita R. Magalon, Axel Léger, Christophe Pereira, Inês a. c. Walburger, Anne Fourmond, Vincent |
author_role |
author |
author2 |
Uzel, Alexandre Broc, Marianne Manuel, Rita R. Magalon, Axel Léger, Christophe Pereira, Inês a. c. Walburger, Anne Fourmond, Vincent |
author2_role |
author author author 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 |
Meneghello, Marta Uzel, Alexandre Broc, Marianne Manuel, Rita R. Magalon, Axel Léger, Christophe Pereira, Inês a. c. Walburger, Anne Fourmond, Vincent |
description |
Metal-based formate dehydrogenases are molybdenum or tungsten-dependent enzymes that catalyze the interconversion between formate and CO2. According to the current consensus, the metal ion of the catalytic center in its active form is coordinated by 6 S (or 5 S and 1 Se) atoms, leaving no free coordination sites to which formate could bind to the metal. Some authors have proposed that one of the active site ligands decoordinates during turnover to allow formate binding. Another proposal is that the oxidation of formate takes place in the second coordination sphere of the metal. Here, we have used electrochemical steady-state kinetics to elucidate the order of the steps in the catalytic cycle of two formate dehydrogenases. Our results strongly support the “second coordination sphere” hypothesis. |
publishDate |
2023 |
dc.date.none.fl_str_mv |
2023-09-30T22:20:29Z 2023-02-01 2023-02-01T00:00:00Z |
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/10362/158534 |
url |
http://hdl.handle.net/10362/158534 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
1433-7851 PURE: 72579828 https://doi.org/10.1002/anie.202212224 |
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.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) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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