Abstract
Radioactive (125)I emits short-range Auger electrons and represents a human health risk when incorporated in thyroglobulin of the thyroid. Quantitative evaluation of this risk can only be realised if local atomic order about iodine in the thyroid is known. Here, extended X-ray absorption fine structure (EXAFS) has been used to probe the local structure about iodine in pure thyroid hormone, thyroxine. These data are consistent with a model where iodine is bound to a single iodinated carbon ring linked to an oxygen atom, similar to a previously published model for monoiodotyrosine, a major iodinated residue in thyroglobulin. Several structural models for the local environment of iodine from rat, human and sheep have been tested and these data are found to be compatible with a slightly modified environment with respect to that found for thyroxine. The best-fit models include the following three components: (i) iodine covalently bonded to a tyrosine ring, as found for thyroxine; (ii) iodine bonded quasi-covalently to a carbonyl ligand in partially filled (50%) sites; (iii) partially filled sites (50-40%) of carbonyl ligands, with oxygen at van der Waals distances from iodine. Advantages of using Fourier-filtered EXAFS for complex crystal structures are discussed.
Paper version not known (
Free)
Published Version
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call