Unraveling the mode of function of the W-containing formate dehydrogenase (Fdh) enzyme

Detalhes bibliográficos
Autor(a) principal: Alves, Guilherme Vilela
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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spelling 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
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url http://hdl.handle.net/10362/142774
dc.language.iso.fl_str_mv eng
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