Aluminum site structure in serum transferrin and lactoferrin revealed by synchrotron radiation X-ray spectroscopy

Biometals. 1997 Oct;10(4):363-7. doi: 10.1023/a:1018345021238.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aluminum / analysis*
  • Aluminum / chemistry
  • Binding Sites
  • Lactoferrin / chemistry*
  • Spectrometry, X-Ray Emission
  • Transferrin / chemistry*

Substances

  • Transferrin
  • Aluminum
  • Lactoferrin