Model peptide studies of Ag + binding sites from the silver resistance protein SilE

Using model peptides, each of the nine MX H or HX M (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.

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Bibliographic Details
Published in:Chemical communications (Cambridge, England) England), 2017-06, Vol.53 (45), p.6105-6108
Main Authors: Chabert, V, Hologne, M, Sénèque, O, Crochet, A, Walker, O, Fromm, K M
Format: Article
Language:English
Subjects:
Binding sites
Buffers
Chemical Sciences
Histidine
Mathematical models
Methionine
Peptides
Proteins
Residues
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Description
Summary:Using model peptides, each of the nine MX H or HX M (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.
ISSN:1359-7345
1364-548X
DOI:10.1039/c7cc02630g