Aluminum site structure in serum transferrin and lactoferrin revealed by synchrotron radiation X-ray spectroscopy.
The Al site structure of serum transferrin and lactoferrin is investigated using X-ray absorption near edge structure (XANES) spectroscopy. Al K-edge spectra in the mono- and dialuminum forms of the proteins have been recorded for the first time. Our results show that the aluminium ion is hexa-coordinated in an octahedral-like symmetry and that the monoaluminum form, where only the C-terminal binding site is saturated, has an increased structural distortion around the metal site.
Congiu-Castellano
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A
Dipartimento di fisica and INFM, Universita' la Sapienza, Roma, Italy. congiu@axcasp.caspur.it
Boffi
F
F
Della Longa
S
S
Giovannelli
A
A
Girasole
M
M
Natali
F
F
Pompa
M
M
Soldatov
A
A
Bianconi
A
A
D000535:Aluminum / Q000032:analysis* / Q000737:chemistry; D001665:Binding Sites; D007781:Lactoferrin / Q000737:chemistry*; D013052:Spectrometry, X-Ray Emission; D014168:Transferrin / Q000737:chemistry*
D014168:Transferrin; D000535:Aluminum; D007781:Lactoferrin