Unraveling the mode of function of the W-containing formate dehydrogenase (Fdh) enzyme
Autor(a) principal: | |
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Data de Publicação: | 2022 |
Tipo de documento: | Dissertação |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10362/142774 |
Resumo: | Anthropogenic CO2 emissions are rising since the Industrial Revolution and, with them, Earth temperature, as its consequences already impact our society, these being a 21st century key challenge. Harnessing millions of years of evolution is a promising way to halt CO2 emissions and possibly revert them. Formate Dehydrogenases (Fdh), especially the Mo and W-de-pendent ones, can efficiently, specifically and reversibly interconvert formate and CO2. Additionally, these enzymes are also relevant in human health with formate being a key metabolite in several diseases. Here, we report the structural characterization of the Desulfovibrio vulgaris FdhAB mutants and in complex with ligands. The results here reported push us one small step closer to an Fdh-based biotechnological solution capable of driving our society towards equilibrium with Nature. |
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Unraveling the mode of function of the W-containing formate dehydrogenase (Fdh) enzymeFormate Dehydrogenase (Fdh)CO2 Enzymatic ReductionMo- and W-EnzymesDesulfovibrio vulgarisX-ray CrystallographyDomínio/Área Científica::Engenharia e Tecnologia::Outras Engenharias e TecnologiasAnthropogenic CO2 emissions are rising since the Industrial Revolution and, with them, Earth temperature, as its consequences already impact our society, these being a 21st century key challenge. Harnessing millions of years of evolution is a promising way to halt CO2 emissions and possibly revert them. Formate Dehydrogenases (Fdh), especially the Mo and W-de-pendent ones, can efficiently, specifically and reversibly interconvert formate and CO2. Additionally, these enzymes are also relevant in human health with formate being a key metabolite in several diseases. Here, we report the structural characterization of the Desulfovibrio vulgaris FdhAB mutants and in complex with ligands. The results here reported push us one small step closer to an Fdh-based biotechnological solution capable of driving our society towards equilibrium with Nature.As emissões antropogénicas de CO2 têm aumentado desde a Revolução Industrial e, com elas, a temperatura da Terra, enquanto as respectivas consequências já têm impacto na nossa sociedade, sendo este um dos maiores desafios do século XXI. Capitalizar milhões de anos de evolução é uma forma promissora de desacelerar as emissões de CO2 e possivelmente revertê-las. As Formato Desidrogenases (Fdh), especificamente as dependentes de Mo ou W, interconvertem formato e CO2 de uma forma eficiente, específica e reversível. Estas enzimas são também relevantes na saúde humana, sendo o formato um metabolito chave em várias doenças. Este trabalho reporta a caracterização estrutural da FdhAB de Desulfovibrio vulgaris, mutantes e em complexo com ligandos. Os resultados reportados colocam-nos um pequeno passo mais perto de uma solução biotecnológica baseada na Fdh capaz de impulsionar a nossa sociedade para um equilíbrio com a Natureza.Mota, CristianoRomão, Maria JoãoRUNAlves, Guilherme Vilela2022-07-282025-06-30T00:00:00Z2022-07-28T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/masterThesisapplication/pdfhttp://hdl.handle.net/10362/142774enginfo:eu-repo/semantics/embargoedAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-03-11T05:20:41Zoai:run.unl.pt:10362/142774Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:50:30.827366Repositório 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 |
Unraveling the mode of function of the W-containing formate dehydrogenase (Fdh) enzyme |
title |
Unraveling the mode of function of the W-containing formate dehydrogenase (Fdh) enzyme |
spellingShingle |
Unraveling the mode of function of the W-containing formate dehydrogenase (Fdh) enzyme Alves, Guilherme Vilela Formate Dehydrogenase (Fdh) CO2 Enzymatic Reduction Mo- and W-Enzymes Desulfovibrio vulgaris X-ray Crystallography Domínio/Área Científica::Engenharia e Tecnologia::Outras Engenharias e Tecnologias |
title_short |
Unraveling the mode of function of the W-containing formate dehydrogenase (Fdh) enzyme |
title_full |
Unraveling the mode of function of the W-containing formate dehydrogenase (Fdh) enzyme |
title_fullStr |
Unraveling the mode of function of the W-containing formate dehydrogenase (Fdh) enzyme |
title_full_unstemmed |
Unraveling the mode of function of the W-containing formate dehydrogenase (Fdh) enzyme |
title_sort |
Unraveling the mode of function of the W-containing formate dehydrogenase (Fdh) enzyme |
author |
Alves, Guilherme Vilela |
author_facet |
Alves, Guilherme Vilela |
author_role |
author |
dc.contributor.none.fl_str_mv |
Mota, Cristiano Romão, Maria João RUN |
dc.contributor.author.fl_str_mv |
Alves, Guilherme Vilela |
dc.subject.por.fl_str_mv |
Formate Dehydrogenase (Fdh) CO2 Enzymatic Reduction Mo- and W-Enzymes Desulfovibrio vulgaris X-ray Crystallography Domínio/Área Científica::Engenharia e Tecnologia::Outras Engenharias e Tecnologias |
topic |
Formate Dehydrogenase (Fdh) CO2 Enzymatic Reduction Mo- and W-Enzymes Desulfovibrio vulgaris X-ray Crystallography Domínio/Área Científica::Engenharia e Tecnologia::Outras Engenharias e Tecnologias |
description |
Anthropogenic CO2 emissions are rising since the Industrial Revolution and, with them, Earth temperature, as its consequences already impact our society, these being a 21st century key challenge. Harnessing millions of years of evolution is a promising way to halt CO2 emissions and possibly revert them. Formate Dehydrogenases (Fdh), especially the Mo and W-de-pendent ones, can efficiently, specifically and reversibly interconvert formate and CO2. Additionally, these enzymes are also relevant in human health with formate being a key metabolite in several diseases. Here, we report the structural characterization of the Desulfovibrio vulgaris FdhAB mutants and in complex with ligands. The results here reported push us one small step closer to an Fdh-based biotechnological solution capable of driving our society towards equilibrium with Nature. |
publishDate |
2022 |
dc.date.none.fl_str_mv |
2022-07-28 2022-07-28T00:00:00Z 2025-06-30T00:00:00Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/masterThesis |
format |
masterThesis |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10362/142774 |
url |
http://hdl.handle.net/10362/142774 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/embargoedAccess |
eu_rights_str_mv |
embargoedAccess |
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 |
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 |
|
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1799138101909520384 |