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|Title:||The iron binding-sites of chicken ovotransferrin|
|Authors:||Lindley, PF;Evans, RW;Garratt, RC;Hasnain, SS|
|subject:||EXAFS spectrum;Diferric chicken ovotransferrin;XANES spectrum;Freeze-drying;Iron-binding sites;Fragmentation|
|Description:||We have shown previously that the EXAFS spectrum of diferric chicken ovotransferrin (Fe2COT) can only be adequately simulated assuming a split first shell co-ordination . EXAFS and XANES spectra of Fe2COT measured in solution and as a freeze-dried powder provide evidence for perturbation of the iron-binding sites on freeze-drying which involves the loss of one of the long (~2.04 Å) first shell ligands (presumably water). Measurement of the XANES of the C-terminal monoferric COT and a C-terminal domain fragment suggests that the metal binding site remains largely unperturbed by the fragmentation process. The possibility of site interaction is briefly discussed.|
We gratefully acknowledge the SERC for financial support and provision of facilities.
|Standard no:||Journal de Physique, 47(C8): 1189-1192, December 1986|
|Appears in Collections:||Dept of Life Sciences Research Papers|
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