Issue 26, 2012

The metal selectivity of a short peptide maquette imitating the high-affinity metal-binding site of E. coli HypB

Abstract

A seven-residue peptide based on the high-affinity metal-binding site of E. coli HypB maintains the nickel-binding activity of the full-length protein. The ability of the peptide to bind transition metals other than nickel was explored, and is discussed in the context of the function of HypB in hydrogenase biosynthesis.

Graphical abstract: The metal selectivity of a short peptide maquette imitating the high-affinity metal-binding site of E. coli HypB

Supplementary files

Article information

Article type
Communication
Submitted
18 Jan 2012
Accepted
24 Feb 2012
First published
28 Feb 2012

Dalton Trans., 2012,41, 7876-7878

The metal selectivity of a short peptide maquette imitating the high-affinity metal-binding site of E. coli HypB

C. D. Douglas, A. V. Dias and D. B. Zamble, Dalton Trans., 2012, 41, 7876 DOI: 10.1039/C2DT30132F

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