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The structure of the copper site in folded and unfolded copper(I) azurin has been investigated by X-ray absorption spectroscopy (XAS). Analysis of the Cu K-edge spectra demonstrates that Cu(I) occupies a trigonal coordination site in the unfolded protein; and EXAFS data indicate a structure with 1.5-2 Cu S(Cl) and 1.5-1 Cu N(O) bonds. It is likely that the cysteine S and one of the two histidine...
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