title: 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.
authors.affiliation: Department of Chemistry, University of Toronto, Toronto, Canada.
authors.forename: Colin D
authors.initials: CD
authors.lastname: Douglas
authors.forename: Alistair V
authors.initials: AV
authors.lastname: Dias
authors.forename: Deborah B
authors.initials: DB
authors.lastname: Zamble
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000378:metabolism*; D019204:GTP-Binding Proteins / Q000378:metabolism*; D010455:Peptides / Q000378:metabolism*; D028561:Transition Elements / Q000737:chemistry / Q000378:metabolism*
chemical_list: D029968:Escherichia coli Proteins; C490324:HypB protein, E coli; D010455:Peptides; D028561:Transition Elements; D019204:GTP-Binding Proteins