CHAPTER 4: Nickel Binding Sites – Coordination Modes and Thermodynamics
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Published:24 Mar 2017
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Special Collection: 2017 ebook collection
M. Rowińska-Żyrek and H. Kozłowski, in The Biological Chemistry of Nickel, ed. D. Zamble, M. Rowińska-Żyrek, and H. Kozlowski, The Royal Society of Chemistry, 2017, pp. 43-59.
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Nickel, the main character of this book, is a key player of several enzymes, present mostly in lower organisms. The metal is completely unnecessary for humans and crucial for the survival and virulence of pathogens, therefore its coordination chemistry could be an excellent therapeutic target. In this chapter, we explain the coordination chemistry of nickel, focusing on its protein binding properties. Detailed descriptions of complex binding modes are intertwined with explorations of chemically fascinating binding sites in bacterial proteins, such as the cysteine-rich or poly-histidine repeats in nickel chaperones of Helicobacter pylori.