Zinc-binding moieties

Figure 1.9 Examples of functionally important intrinsic metal atoms in proteins, (a) The di-iron center of the enzyme ribonucleotide reductase. Two iron atoms form a redox center that produces a free radical in a nearby tyrosine side chain. The iron atoms are bridged by a glutamic acid residue and a negatively charged oxygen atom called a p-oxo bridge. The coordination of the iron atoms is completed by histidine, aspartic acid, and glutamic acid side chains as well as water molecules, (b) The catalytically active zinc atom in the enzyme alcohol dehydrogenase. The zinc atom is coordinated to the protein by one histidine and two cysteine side chains. During catalysis zinc binds an alcohol molecule in a suitable position for hydride transfer to the coenzyme moiety, a nicotinamide, [(a) Adapted from P. Nordlund et al., Nature 345 593-598, 1990.)...

The open-isomer of DTE having two zinc porphyrin moieties could form coordination complex with 4,4-bipyridyl like a tweezer (see Scheme 4), but the closed isomer could not bind cooperatively because of its structural rigidity. The different binding behavior of ZnP-DTE-ZnP with 4,4-bipyridyl was though to make the photo-control of affinity to guest molecules possible. 

A conjugate between thiazole orange and the zinc-finger moiety of glucocorticoid receptor DNA-binding domain (GR-DBD) has been synthe-... 

HDACs are a family of enzymes that catalyze the deacetylation of lysine side chain in chromatin. These enzymes are involved in a wide range of biological processes such as cell differentiation, proliferation, angiogenesis, and apoptosis. HDAC inhibitors have been clinically validated as a therapeutic strategy for cancer treatment. This topic has been covered by critical reviews [55-58]. The classic pharmacophore for HDAC inhibitors consists of three distinct structural motifs the zinc-binding group, a hydrophobic linker, and a recognition cap moiety. 

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