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Campo DC | Valor | Lengua/Idioma |
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dc.contributor.author | Benchoam, Dayana | - |
dc.contributor.author | Cuevasanta, Ernesto | - |
dc.contributor.author | Julió Plana, Laia | - |
dc.contributor.author | Capece, Luciana | - |
dc.contributor.author | Banerjee, Ruma | - |
dc.contributor.author | Álvarez, Beatriz | - |
dc.date.accessioned | 2022-08-30T14:36:33Z | - |
dc.date.available | 2022-08-30T14:36:33Z | - |
dc.date.issued | 2021 | - |
dc.identifier.citation | Benchoam, D, Cuevasanta, E, Julió Plana, L [y otros autores]. "Heme-Thiolate perturbation in cystathionine β-Synthase by mercury compounds". ACS Omega. [en línea] 2021, 6(3): 2192-2205. 14 h. DOI: 10.1021/acsomega.0c05475. | es |
dc.identifier.issn | 2470-1343 | - |
dc.identifier.uri | https://hdl.handle.net/20.500.12008/33431 | - |
dc.description.abstract | Cystathionine β-synthase (CBS) is an enzyme involved in sulfur metabolism that catalyzes the pyridoxal phosphate-dependent condensation of homocysteine with serine or cysteine to form cystathionine and water or hydrogen sulfide (H2S), respectively. CBS possesses a b-type heme coordinated by histidine and cysteine. Fe(III)-CBS is inert toward exogenous ligands, while Fe(II)-CBS is reactive. Both Fe(III)- and Fe(II)-CBS are sensitive to mercury compounds. In this study, we describe the kinetics of the reactions with mercuric chloride (HgCl2) and p-chloromercuribenzoic acid. These reactions were multiphasic and resulted in five-coordinate CBS lacking thiolate ligation, with six-coordinate species as intermediates. Computational QM/MM studies supported the feasibility of formation of species in which the thiolate is proximal to both the iron ion and the mercury compound. The reactions of Fe(II)-CBS were faster than those of Fe(III)-CBS. The observed rate constants of the first phase increased hyperbolically with concentration of the mercury compounds, with limiting values of 0.3–0.4 s–1 for Fe(III)-CBS and 40 ± 4 s–1 for Fe(II)-CBS. The data were interpreted in terms of alternative models of conformational selection or induced fit. Exposure of Fe(III)-CBS to HgCl2 led to heme release and activity loss. Our study reveals the complexity of the interactions between mercury compounds and CBS. | es |
dc.format.extent | 14 h | es |
dc.format.mimetype | application/pdf | es |
dc.language.iso | en | es |
dc.publisher | American Chemical Society | es |
dc.relation.ispartof | ACS Omega, 2021, 6(3): 2192-2205. | es |
dc.rights | Las obras depositadas en el Repositorio se rigen por la Ordenanza de los Derechos de la Propiedad Intelectual de la Universidad de la República.(Res. Nº 91 de C.D.C. de 8/III/1994 – D.O. 7/IV/1994) y por la Ordenanza del Repositorio Abierto de la Universidad de la República (Res. Nº 16 de C.D.C. de 07/10/2014) | es |
dc.subject | Bioinorganic chemistry | es |
dc.subject | Kinetic parameters | es |
dc.subject | Ligands | es |
dc.subject | Mercury | es |
dc.title | Heme-Thiolate perturbation in cystathionine β-Synthase by mercury compounds | es |
dc.type | Artículo | es |
dc.contributor.filiacion | Benchoam Dayana, Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Ecología y Ciencias Ambientales. | - |
dc.contributor.filiacion | Cuevasanta Ernesto, Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Ecología y Ciencias Ambientales. | - |
dc.contributor.filiacion | Julió Plana Laia | - |
dc.contributor.filiacion | Capece Luciana | - |
dc.contributor.filiacion | Banerjee Ruma | - |
dc.contributor.filiacion | Álvarez Beatriz, Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Ecología y Ciencias Ambientales. | - |
dc.rights.licence | Licencia Creative Commons Atribución - No Comercial - Sin Derivadas (CC - By-NC-ND 4.0) | es |
dc.identifier.doi | 10.1021/acsomega.0c05475 | - |
Aparece en las colecciones: | Publicaciones académicas y científicas - Facultad de Ciencias |
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