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Nickel Metalloregulators and Chaperones

Department of Chemistry, Salve Regina University, Newport, RI 02840, USA
Inorganics 2019, 7(8), 104; https://doi.org/10.3390/inorganics7080104
Received: 11 June 2019 / Revised: 13 August 2019 / Accepted: 14 August 2019 / Published: 19 August 2019
(This article belongs to the Special Issue Bioinorganic Chemistry of Nickel)
Nickel is essential for the survival of many pathogenic bacteria. E. coli and H. pylori require nickel for [NiFe]-hydrogenases. H. pylori also requires nickel for urease. At high concentrations nickel can be toxic to the cell, therefore, nickel concentrations are tightly regulated. Metalloregulators help to maintain nickel concentration in the cell by regulating the expression of the genes associated with nickel import and export. Nickel import into the cell, delivery of nickel to target proteins, and export of nickel from the cell is a very intricate and well-choreographed process. The delivery of nickel to [NiFe]-hydrogenase and urease is complex and involves several chaperones and accessory proteins. A combination of biochemical, crystallographic, and spectroscopic techniques has been utilized to study the structures of these proteins, as well as protein–protein interactions resulting in an expansion of our knowledge regarding how these proteins sense and bind nickel. In this review, recent advances in the field will be discussed, focusing on the metal site structures of nickel bound to metalloregulators and chaperones. View Full-Text
Keywords: nickel; metalloregulator; chaperone; [NiFe]-hydrogenase; urease nickel; metalloregulator; chaperone; [NiFe]-hydrogenase; urease
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MDPI and ACS Style

Higgins, K. Nickel Metalloregulators and Chaperones. Inorganics 2019, 7, 104.

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