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CommunicationsNickel Binding and [NiFe]-Hydrogenase Maturation by the Metallochaperone SlyD with a Single Metal-Binding Site in Escherichia coli.

Posted from Journal of Molecular Biology 99 days ago
Molecular Biology : Molecular Biology Journals

Publication Date: 2012 Jan 30 PMID: 22310044Authors: Kaluarachchi, H. - Altenstein, M. - Sugumar, S. R. - Balbach, J. - Zamble, D. B. - Haupt, C.Journal: J Mol BiolSlyD (sensitive to lysis D) is a nickel metallochaperone involved in the maturation of [NiFe]-hydrogenases in Escherichia coli (E. coli) and specifically contributes to the nickel delivery step during enzyme biosynthesis. This protein contains a C-terminal metal-binding domain that is rich in potential metal-binding residues that enable SlyD to bind multiple nickel ions with high affinity. The SlyD homolog from Thermus thermophilus ... (original story)