Electrochemical characterization of a family AA10 LPMO and the impact of residues shaping the copper site on reactivity
| Autor(a) principal: | |
|---|---|
| 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/10362/145850 |
Resumo: | This work was supported by the OXYMOD project funded by the Research Council of Norway with grant number 269408. CNC thanks FCT (Fundação para a Ciência e Tecnologia) for funding through program DL 57/2016 – Norma transitória |
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Electrochemical characterization of a family AA10 LPMO and the impact of residues shaping the copper site on reactivityLPMOEnzymesMutantsCopper centresElectrochemistryDirect electron transferBiochemistryBiophysicsStructural BiologyElectrochemistryInorganic ChemistrySDG 7 - Affordable and Clean EnergySDG 9 - Industry, Innovation, and InfrastructureSDG 12 - Responsible Consumption and ProductionSDG 15 - Life on LandThis work was supported by the OXYMOD project funded by the Research Council of Norway with grant number 269408. CNC thanks FCT (Fundação para a Ciência e Tecnologia) for funding through program DL 57/2016 – Norma transitóriaResearch on enzymes for lignocellulose biomass degradation has progressively increased in recent years due to the interest in taking advantage of this natural resource. Among these enzymes are the lytic polysaccharide monooxygenases (LPMOs) that oxidatively depolymerize crystalline cellulose using a reactive oxygen species generated in a reduced mono‑copper active site. The copper site comprises of a highly conserved histidine-brace, providing three equatorial nitrogen ligands, whereas less conserved residues close to the copper contribute to shaping and confining the site. The catalytic copper site is exposed to the solvent and to the crystalline substrates, and as so, the influence of the copper environment on LPMO properties, including the redox potential, is of great interest. In the current work, a direct electrochemical study of an LPMO (ScLPMO10C) was conducted allowing to retrieve kinetic and thermodynamic data associated with the redox transition in the catalytic centre. Moreover, two residues that do not bind to the copper but shape the copper sites were mutated, and the properties of the mutants were compared with those of the wild-type enzyme. The direct electrochemical studies, using cyclic voltammetry, yielded redox potentials in the +200 mV range, well in line with LPMO redox potentials determined by other methods. Interestingly, while the mutations hardly affected the formal redox potential of the enzyme, they drastically affected the reactivity of the copper site and enzyme functionality.LAQV@REQUIMTERUNCordas, Cristina M.Valério, Gabriel de NóbregaStepnov, AntonKommedal, EirikR. Kjendseth, AsmundForsberg, ZarahEijsink, Vincent G. H.Moura, José J. G.2024-12-01T01:31:49Z2023-012023-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article9application/pdfhttp://hdl.handle.net/10362/145850eng0162-0134PURE: 47525702https://doi.org/10.1016/j.jinorgbio.2022.112056info: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:RCAAP2024-12-02T01:34:55Zoai:run.unl.pt:10362/145850Portal AgregadorONGhttps://www.rcaap.pt/oai/openairemluisa.alvim@gmail.comopendoar:71602024-12-02T01:34:55Repositório 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 characterization of a family AA10 LPMO and the impact of residues shaping the copper site on reactivity |
| title |
Electrochemical characterization of a family AA10 LPMO and the impact of residues shaping the copper site on reactivity |
| spellingShingle |
Electrochemical characterization of a family AA10 LPMO and the impact of residues shaping the copper site on reactivity Cordas, Cristina M. LPMO Enzymes Mutants Copper centres Electrochemistry Direct electron transfer Biochemistry Biophysics Structural Biology Electrochemistry Inorganic Chemistry SDG 7 - Affordable and Clean Energy SDG 9 - Industry, Innovation, and Infrastructure SDG 12 - Responsible Consumption and Production SDG 15 - Life on Land |
| title_short |
Electrochemical characterization of a family AA10 LPMO and the impact of residues shaping the copper site on reactivity |
| title_full |
Electrochemical characterization of a family AA10 LPMO and the impact of residues shaping the copper site on reactivity |
| title_fullStr |
Electrochemical characterization of a family AA10 LPMO and the impact of residues shaping the copper site on reactivity |
| title_full_unstemmed |
Electrochemical characterization of a family AA10 LPMO and the impact of residues shaping the copper site on reactivity |
| title_sort |
Electrochemical characterization of a family AA10 LPMO and the impact of residues shaping the copper site on reactivity |
| author |
Cordas, Cristina M. |
| author_facet |
Cordas, Cristina M. Valério, Gabriel de Nóbrega Stepnov, Anton Kommedal, Eirik R. Kjendseth, Asmund Forsberg, Zarah Eijsink, Vincent G. H. Moura, José J. G. |
| author_role |
author |
| author2 |
Valério, Gabriel de Nóbrega Stepnov, Anton Kommedal, Eirik R. Kjendseth, Asmund Forsberg, Zarah Eijsink, Vincent G. H. Moura, José J. G. |
| author2_role |
author author author author author author author |
| dc.contributor.none.fl_str_mv |
LAQV@REQUIMTE RUN |
| dc.contributor.author.fl_str_mv |
Cordas, Cristina M. Valério, Gabriel de Nóbrega Stepnov, Anton Kommedal, Eirik R. Kjendseth, Asmund Forsberg, Zarah Eijsink, Vincent G. H. Moura, José J. G. |
| dc.subject.por.fl_str_mv |
LPMO Enzymes Mutants Copper centres Electrochemistry Direct electron transfer Biochemistry Biophysics Structural Biology Electrochemistry Inorganic Chemistry SDG 7 - Affordable and Clean Energy SDG 9 - Industry, Innovation, and Infrastructure SDG 12 - Responsible Consumption and Production SDG 15 - Life on Land |
| topic |
LPMO Enzymes Mutants Copper centres Electrochemistry Direct electron transfer Biochemistry Biophysics Structural Biology Electrochemistry Inorganic Chemistry SDG 7 - Affordable and Clean Energy SDG 9 - Industry, Innovation, and Infrastructure SDG 12 - Responsible Consumption and Production SDG 15 - Life on Land |
| description |
This work was supported by the OXYMOD project funded by the Research Council of Norway with grant number 269408. CNC thanks FCT (Fundação para a Ciência e Tecnologia) for funding through program DL 57/2016 – Norma transitória |
| publishDate |
2023 |
| dc.date.none.fl_str_mv |
2023-01 2023-01-01T00:00:00Z 2024-12-01T01:31:49Z |
| 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/10362/145850 |
| url |
http://hdl.handle.net/10362/145850 |
| dc.language.iso.fl_str_mv |
eng |
| language |
eng |
| dc.relation.none.fl_str_mv |
0162-0134 PURE: 47525702 https://doi.org/10.1016/j.jinorgbio.2022.112056 |
| dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
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openAccess |
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9 application/pdf |
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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 |
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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 |
| repository.mail.fl_str_mv |
mluisa.alvim@gmail.com |
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1817545900262686720 |