Abstract

Following the discovery of the first specific and essential role of nickel in biology in 1975 (the dinuclear active site of the enzyme urease) [...]

Highlights

  • The understanding of the biological role of nickel from the inorganic chemistry side is reviewed on a theoretical basis by Siegbahn et al [2], who discuss the enzyme mechanisms, including the canonical mechanism of urease, in view of the recently reported crystal structure of the enzyme-substrate complex [3]

  • The knowledge of proteins involved in cellular nickel trafficking is summarized by Higgins in a review [5], which is complemented by a second monographic article by Nim and Wong [6], that focuses on the maturation of the nickel enzyme urease as a paradigmatic example of how cells balance nickel essentiality and toxicity. These two reviews are augmented by two original research papers on this aspect of the nickel bioinorganic chemistry field: the paper by Alfano et al [7] is focused on CooJ, an accessory protein necessary for the maturation of the nickel-dependent enzyme carbon monoxide dehydrogenase, while the paper by Barchi and Musiani [8] describes the structure-function relationships in InrS, a nickel-dependent transcription factor from cyanobacteria

  • Other reviews in this issue focus on aspects of nickel in human health, with the goal of making this literature more accessible to the bioinorganic community

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Summary

Introduction

The understanding of the biological role of nickel from the inorganic chemistry side is reviewed on a theoretical basis by Siegbahn et al [2], who discuss the enzyme mechanisms, including the canonical mechanism of urease, in view of the recently reported crystal structure of the enzyme-substrate complex [3]. This chemistry is further elucidated by original contributions on the pH dependence of binuclear nickel peptide complexes by Keegan et al [4].

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