title: Comparative XANES study of serotransferrin and ovotransferrin at Cu K-edge: evidence of interactions among the metal sites.
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-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.
authors: Dipartimento di Fisica and INFM, Università La Sapienza, Roma.
authors: F
authors: F
authors: Boffi
authors: I
authors: I
authors: Ascone
authors: A
authors: A
authors: Varoli Piazza
authors: M
authors: M
authors: Girasole
authors: S
authors: S
authors: Della Longa
authors: A
authors: A
authors: Giovannelli
authors: A
authors: A
authors: Congiu Castellano
mesh_terms: D000818:Animals; D001665:Binding Sites; D002645:Chickens; D003207:Conalbumin / Q000737:chemistry*; D003300:Copper / Q000737:chemistry*; D006801:Humans; D010446:Peptide Fragments / Q000737:chemistry; D013052:Spectrometry, X-Ray Emission; D013056:Spectrophotometry, Ultraviolet; D014168:Transferrin / Q000737:chemistry*
chemical_list: D010446:Peptide Fragments; D014168:Transferrin; D003207:Conalbumin; D003300:Copper