Comparative XANES study of serotransferrin and ovotransferrin at Cu K-edge: evidence of interactions among the metal sites.

Boffi, F; Ascone, I; Varoli Piazza, A; Girasole, M; Della Longa, S; Giovannelli, A; Congiu Castellano, A

Boffi, F; Ascone, I; Varoli Piazza, A; Girasole, M; Della Longa, S; Giovannelli, A; Congiu Castellano, A.

Afiliación

Boffi F; Dipartimento di Fisica and INFM, Università La Sapienza, Roma.

Biometals ; 13(3): 217-22, 2000 Sep.

Article en En | MEDLINE | ID: mdl-11127893

RESUMEN

The Cu site structure of human serotransferrin and hen ovotransferrin using XANES spectroscopy has been investigated. Although the transferrin family proteins have been extensively studied, the results reported herein are the first concerning the structure of the metal site in C-terminal and N-terminal in the whole protein. Our structural data show that these proteins differ with regard to the independence of the two binding sites and the geometry of copper coordination, ranging from a poorly to a significantly distorted octahedron.

Asunto(s)

Conalbúmina/química; Cobre/química; Transferrina/química; Animales; Sitios de Unión; Pollos; Humanos; Fragmentos de Péptidos/química; Espectrometría por Rayos X; Espectrofotometría Ultravioleta

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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Transferrina / Conalbúmina / Cobre Límite: Animals / Humans Idioma: En Revista: Biometals Asunto de la revista: BIOQUIMICA Año: 2000 Tipo del documento: Article Pais de publicación: Países Bajos

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