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The acid/base chemistry and the zinc complexation of the four dipeptides H-HisHis-OH, H-HisHis-OEt, Ac-HisHis-OH and Ac-HisHis-OEt were investigated by potentiometric methods. 1:1 (zinc:dipeptide) complexes prevail in solution, and those complexes that could be isolated on a preparative scale also have 1:1 compositions. The stability data confirm that exclusive zinc-imidazole(histidine) coordination is weak, and additional effects are essential to effect the high preference of zinc for histidine in proteins. A comparison of the stability data for zinc complexes of all dipeptides made up solely from histidine and/or cysteine reveals systematic trends and allows a parameterization of the log β values.
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Vogler et al. (2002) studied this question.
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