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Cys34 in domain I of the three-domain serum protein albumin is the bind-ing site for a wide variety of biologically and clinically important smallmolecules, provides antioxidant activity, and constitutes the largest portionof free thiol in blood. Analysis of X-ray structures of albumin reveals thatthe loop containing Tyr84 occurs in multiple conformations. In structureswhere the loop is well defined, there appears to be an H-bond between theOH of Tyr84 and the sulfur of Cys34. We show that the reaction of 5,5¢-di-thiobis(2-nitrobenzoic acid) (DTNB) with Tyr84Phe mutant albumin isapproximately four times faster than with the wild-type protein betweenpH 6 and pH 8....
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Báo cáo khoa học: Role of Tyr84 in controlling the reactivity of Cys34 of human albumin
