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

Citation
F. Boffi et al., Comparative XANES study of serotransferrin and ovotransferrin at CuK-edge:evidence of interactions among the metal sites, BIOMETALS, 13(3), 2000, pp. 217-222
Citations number
26
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOMETALS
ISSN journal
09660844 → ACNP
Volume
13
Issue
3
Year of publication
2000
Pages
217 - 222
Database
ISI
SICI code
0966-0844(200009)13:3<217:CXSOSA>2.0.ZU;2-4
Abstract
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-termi nal in the whole protein. Our structural data show that these proteins diff er with regard to the independence of the two binding sites and the geometr y of copper coordination, ranging from a poorly to a significantly distorte d octahedron.