Jump to main content
Jump to site search

Issue 26, 2012
Previous Article Next Article

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

Author affiliations

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

Back to tab navigation

Supplementary files

Article information


Submitted
18 Jan 2012
Accepted
24 Feb 2012
First published
28 Feb 2012

Dalton Trans., 2012,41, 7876-7878
Article type
Communication

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

Social activity

Search articles by author

Spotlight

Advertisements