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• W2319312964 abstract "Iron K-edge extended-X-ray-absorption-fine-structure (e.x.a.f.s.) spectra were recorded for diferric human and rabbit serum transferrins and for diferric chicken ovotransferrin in aqueous solution; for ovotransferrin e.x.a.f.s. spectra from the N-terminal and C-terminal domain fragments were also measured. The overall spectral profiles closely resemble one another, indicating similar iron-binding sites. The simulation of the diferric ovotransferrin spectrum suggests a first co-ordination shell consisting of six low-Z ligands (nitrogen/oxygen), two ligands at a distance of approx. 0.185 nm (1.85 A) and four ligands at approx. 0.204 nm (2.04 A). The two shorter distances may correspond to Fe-O (tyrosine), whereas the longer distance is consistent with Fe-N (histidine) and Fe-O (water). Detailed analysis of the spectra of the N-terminal and C-terminal fragments indicates a difference in the short ligand distance." @default.
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• W2319312964 date "1986-01-15" @default.
• W2319312964 modified "2023-09-25" @default.
• W2319312964 title "An extended-X-ray-absorption-fine-structure investigation of diferric transferrins and their iron-binding fragments" @default.
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• W2319312964 doi "https://doi.org/10.1042/bj2330479" @default.
• W2319312964 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1153050" @default.
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