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Campo DC | Valor | Lengua/Idioma |
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dc.contributor.author | Freeman, Samuel L. | - |
dc.contributor.author | Skafar Amen, Vera | - |
dc.contributor.author | Kwon, Hanna | - |
dc.contributor.author | Fielding, Alistair J. | - |
dc.contributor.author | Moody, Peter C. E. | - |
dc.contributor.author | Martínez, Alejandra | - |
dc.contributor.author | Issoglio, Federico M. | - |
dc.contributor.author | Inchausti, Lucas | - |
dc.contributor.author | Smircich, Pablo | - |
dc.contributor.author | Zeida, Ari | - |
dc.contributor.author | Piacenza, Lucía | - |
dc.contributor.author | Radi, Rafael | - |
dc.contributor.author | Raven, Emma L. | - |
dc.date.accessioned | 2023-07-27T14:05:47Z | - |
dc.date.available | 2023-07-27T14:05:47Z | - |
dc.date.issued | 2022 | - |
dc.identifier.citation | Freeman, S, Skafar Amen, V, Kwon, H, [y otros autores]. "Crystal structure of Trypanosoma cruzi heme peroxidase and characterization of its substrate specificity and compound I intermediate". Journal of Biological Chemistry. [en línea] 2022, 298(8): 102204. 10 h. DOI: 10.1016/j.jbc.2022.102204 | es |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | https://hdl.handle.net/20.500.12008/38476 | - |
dc.description.abstract | The protozoan parasite Trypanosoma cruzi is the causative agent of American trypanosomiasis, otherwise known as Chagas disease. To survive in the host, the T. cruzi parasite needs antioxidant defense systems. One of these is a hybrid heme peroxidase, the T. cruzi ascorbate peroxidase-cytochrome c peroxidase enzyme (TcAPx-CcP). TcAPx-CcP has high sequence identity to members of the class I peroxidase family, notably ascorbate peroxidase (APX) and cytochrome c peroxidase (CcP), as well as a mitochondrial peroxidase from Leishmania major (LmP). The aim of this work was to solve the structure and examine the reactivity of the TcAPx-CcP enzyme. Low temperature electron paramagnetic resonance spectra support the formation of an exchange-coupled [Fe(IV)=O Trp233•+] compound I radical species, analogous to that used in CcP and LmP. We demonstrate that TcAPx-CcP is similar in overall structure to APX and CcP, but there are differences in the substrate-binding regions. Furthermore, the electron transfer pathway from cytochrome c to the heme in CcP and LmP is preserved in the TcAPx-CcP structure. Integration of steady state kinetic experiments, molecular dynamic simulations, and bioinformatic analyses indicates that TcAPx-CcP preferentially oxidizes cytochrome c but is still competent for oxidization of ascorbate. The results reveal that TcAPx-CcP is a credible cytochrome c peroxidase, which can also bind and use ascorbate in host cells, where concentrations are in the millimolar range. Thus, kinetically and functionally TcAPx-CcP can be considered a hybrid peroxidase. | es |
dc.format.extent | 10 h. | es |
dc.format.mimetype | application/pdf | es |
dc.language.iso | en_US | es |
dc.publisher | Elsevier Inc. | es |
dc.relation.ispartof | Journal of Biological Chemistry, 2022, 298(8): 102204. | 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 | Peroxidase | es |
dc.subject | Chagas disease | es |
dc.subject | Ascorbate | es |
dc.subject | Cytochrome C. | es |
dc.subject | Heme | es |
dc.subject | Oxidants | es |
dc.title | Crystal structure of Trypanosoma cruzi heme peroxidase and characterization of its substrate specificity and compound I intermediate | es |
dc.type | Artículo | es |
dc.contributor.filiacion | Freeman Samuel L. | - |
dc.contributor.filiacion | Skafar Amen Vera, Universidad de la República (Uruguay). Facultad de Medicina. | - |
dc.contributor.filiacion | Kwon Hanna | - |
dc.contributor.filiacion | Fielding Alistair J. | - |
dc.contributor.filiacion | Moody Peter C. E. | - |
dc.contributor.filiacion | Martínez Alejandra, Universidad de la República (Uruguay). Facultad de Medicina. | - |
dc.contributor.filiacion | Issoglio Federico M. | - |
dc.contributor.filiacion | Inchausti Lucas, Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología. | - |
dc.contributor.filiacion | Smircich Pablo, Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología. | - |
dc.contributor.filiacion | Zeida Ari, Universidad de la República (Uruguay). Facultad de Medicina. | - |
dc.contributor.filiacion | Piacenza Lucía, Universidad de la República (Uruguay). Facultad de Medicina. | - |
dc.contributor.filiacion | Radi Rafael, Universidad de la República (Uruguay). Facultad de Medicina. | - |
dc.contributor.filiacion | Raven Emma L. | - |
dc.rights.licence | Licencia Creative Commons Atribución (CC - By 4.0) | es |
dc.identifier.doi | 10.1016/j.jbc.2022.102204 | - |
Aparece en las colecciones: | Publicaciones académicas y científicas - Facultad de Ciencias |
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