Iron and copper K-edge XAS study of serotransferrin and ovotransferrin.
The active metal site structure of transferrin with iron and copper atoms is investigated using metal K-XANES. Theoretical analysis of experimental data has been performed on the basis of full multiple-scattering theory. This approach made it possible to study the origin of XANES fine details and to investigate the local structure around active metal sites. A deep insight into the local structure and electronic subsystem of Fe, Cu transferrins is obtained. For example, in the case of Cu substitution of Fe in the active centre, the best fit of theoretical spectra to experiment has been obtained for distances 3% smaller between the Cu atom and the nearest neighbours.
Boffi
F
F
Unita' di Roma La Sapienza, Dipartimento di Fisica, Rome, Italy.
Congiu-Castellano
A
A
Varoli-Piazza
A
A
Della Longa
S
S
Girasole
S M
SM
Yalovega
G
G
Soldatov
A V
AV
D000818:Animals; D001665:Binding Sites; D002645:Chickens; D003207:Conalbumin / Q000737:chemistry*; D003300:Copper / Q000737:chemistry*; D005260:Female; D006801:Humans; D007501:Iron / Q000737:chemistry*; D013052:Spectrometry, X-Ray Emission / Q000379:methods; D014168:Transferrin / Q000737:chemistry*
D014168:Transferrin; D003207:Conalbumin; D003300:Copper; D007501:Iron