46Table 2.1 The typical coordination geometry of NO complexes predicted by the Enemark-Feltham electron counting formalism. Coordination number (CN) Idealized geometry CN = 4 CN = 5 CN = 6

The central dogma is the core aspect of biological system regulation, receiving much attention from the field of biological chemistry. One of the main regulators of transcription and translation processes is the zinc finger (ZF) proteins, one or more domains of which coordinate with a zinc ion to interact with their binding partner. ZFs are modular domains that function independently in the presence of Zn 2+ through the generation of short secondary structures via zinc ion coordination, which generate hydrogen bonds, despite being considered structural domains. In this review, structural and functional characteristics of ZF domains will be presented from the perspective of inorganic biochemistry. The major role of ZF domains in the central dogma involves transcriptional regulation through interactions with DNA and translational regulation through the generation of complexes with RNA. These findings indicate that the triggering many biological events can be explained by the coordination and biophysical chemistry of ZFs.

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Copper is utilized as a catalytic metal center in a variety of enzymes involved in oxidation–reduction processes. The Cu(I) and Cu(II) oxidation states are readily accessible and interconvertible under physiological conditions via oxidants (ie, O 2 ) or reducing agents such as ascorbic acid or glutathione. The important chemical transformations that these enzymes are responsible for include dioxygen processing as well as nitrogen oxide (NOx) conversions. The active site structures and catalytic mechanisms of the most well‐studied copper enzymes are described. The contributions to the understanding of enzyme function obtained from biomimetic studies using synthetic copper complexes of most relevance to the active site features have also been highlighted.