Literature DB >> 22415482

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

Colin D Douglas1, Alistair V Dias, Deborah B Zamble.   

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.

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Year:  2012        PMID: 22415482     DOI: 10.1039/c2dt30132f

Source DB:  PubMed          Journal:  Dalton Trans        ISSN: 1477-9226            Impact factor:   4.390


  4 in total

1.  High-affinity metal binding by the Escherichia coli [NiFe]-hydrogenase accessory protein HypB is selectively modulated by SlyD.

Authors:  Mozhgan Khorasani-Motlagh; Michael J Lacasse; Deborah B Zamble
Journal:  Metallomics       Date:  2017-05-24       Impact factor: 4.526

2.  Bimodal Nickel-Binding Site on Escherichia coli [NiFe]-Hydrogenase Metallochaperone HypA.

Authors:  Michael J Lacasse; Kelly L Summers; Mozhgan Khorasani-Motlagh; Graham N George; Deborah B Zamble
Journal:  Inorg Chem       Date:  2019-07-05       Impact factor: 5.165

3.  Metal transfer within the Escherichia coli HypB-HypA complex of hydrogenase accessory proteins.

Authors:  Colin D Douglas; Thanh T Ngu; Harini Kaluarachchi; Deborah B Zamble
Journal:  Biochemistry       Date:  2013-08-22       Impact factor: 3.162

4.  A new approach to biomining: Bioengineering surfaces for metal recovery from aqueous solutions.

Authors:  Jesica Urbina; Advait Patil; Kosuke Fujishima; Ivan G Paulino-Lima; Chad Saltikov; Lynn J Rothschild
Journal:  Sci Rep       Date:  2019-11-11       Impact factor: 4.379

  4 in total

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