Chabert V, Hologne M, Sénèque O, Crochet A, Walker O, Fromm K M
Univ. Fribourg, Department of Chemistry, Chemin du Musée 9, 1700 Fribourg, Switzerland.
Chem Commun (Camb). 2017 Jun 1;53(45):6105-6108. doi: 10.1039/c7cc02630g.
Using model peptides, each of the nine MXH or HXM (n = 1, 2) motifs of the silver resistance protein SilE has been shown to coordinate to one Ag ion by its histidine and methionine residues with K in the μM range. This suggests an Ag buffering role for SilE in the case of high Ag overload.
利用模型肽已表明,抗银蛋白SilE的九个MXH或HXM(n = 1, 2)基序中的每一个都通过其组氨酸和甲硫氨酸残基与一个银离子配位,其平衡常数K在微摩尔范围内。这表明在银严重过载的情况下,SilE具有银缓冲作用。