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An x ray absorption study of the bi nuclear iron center in deoxy hem erythrin



An x ray absorption study of the bi nuclear iron center in deoxy hem erythrin



Journal of the American Chemical Society 105(7): 1919-1923



New EXAFS [extended X-ray absorption fine structure] data at 80.degree. K obtained on deoxyhemerythrin [from Phascolopsis gouldii] in solution reveal an iron-iron peak at a separation of 3.13 .+-. 0.03 .ANG. A repeat of measurements at 300.degree. K shows the iron-iron peak greatly reduced, confirming the hypothesis of increased relative thermal motion of the 2 iron atoms from the loss of the .mu.-oxo bridge. The signal from the 1st shell of ligands around the iron atoms was analyzed by using a difference spectrum vs. oxyhemerythrin, since rearrangements were expected in only a few ligands. The 9 ligands between the irons and the protein remain unchanged, the bound dioxygen is replaced by hydroxide, and the short bond to the bridging oxygen is broken, leaving it bound to 1 iron. Thus, 1 iron becomes 5-coordinate; the other remains 6-coordinate. Details of this analysis are given and the results discussed in light of the information available from other sources.

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Accession: 004735638

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