Transition Metal Coordination Chemistry and Nickel-Dependent Enzyme Mechanisms
This community synthesizes and characterizes coordination complexes of transition metals, with a specific focus on nickel, cobalt, and copper, while also investigating the structural and mechanistic roles of nickel in biological enzymes such as urease and nitrile hydratase.
The recurring title phrases and words highlight a dual focus: the synthesis, crystal structure determination, and thermal decomposition of metal complexes (particularly nickel, cobalt, and copper), and the study of nickel-dependent enzymes including urease, nitrile hydratase, and acetyl-CoA synthase. Key methods include Hirshfeld surface analysis, electron transfer studies, and the characterization of ligand binding and metal ion coordination. The work frequently addresses the interaction between metal ions and biological systems, such as the inhibition of urease activity and the role of nickel in Helicobacter pylori and other microorganisms.
This research constitutes 3.3% of all tracked cobalt research and 1.6% of all tracked nickel research, with the largest paper counts found in cobalt (4,734 papers) and nickel (3,163 papers) studies.
The community comprises 15,284 papers, publishing most frequently in Inorganic Chemistry, Inorganica Chimica Acta, and the Bulletin of the Chemical Society of Japan.
Recent work continues to explore the fundamentals of mixed-valency in multinuclear nickel complexes and the structural insights into cobalt metallochaperone-mediated maturation of nitrile hydratases, alongside the discovery of new nickel enzyme families catalyzing intermolecular hydride shuttling.