Aluminum site structure in serum transferrin and lactoferrin revealed by synchrotron radiation X-ray spectroscopy |
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| Authors: | A. Congiu-Castellano F. Boffi S. Della Longa A. Giovannelli M. Girasole F. Natali M. Pompa A. Soldatov A. Bianconi |
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| Affiliation: | (1) Dipartimento di Fisica and INFM, Universita!["rsquo"]("/content/v7306ph471800048/xlarge8217.gif") la Sapienza, Roma, Italy;(2) Dipartimento di Medicina Sperimentale and INFM, Universita dellAquila, Roma, Italy;(3) Department of Physics, Rostov University, Rostov-Na-Donu, Russia |
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| Abstract: | ![]()
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. |
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| Keywords: | synchrotron radiation transferrins X-ray spectroscopy |
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