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The known Ni enzymes now include ureases, hydrogenases, carbon monoxide dehydrogenases, acetyl coenzyme A synthases, methyl coenzyme M reductases and superoxide dismutases. These enzymes employ Ni in roles varying from Lewis acid sites to involvement in redox catalysis. In addition, mechanisms involving proteins that specifically bind Ni have evolved for the acquisition, transport, and incorporation...
The combination of a pterin and a transition metal in many enzymes is the motivation for exploring the chemistry of pteridine complexes in detail. Unlike other biological ligands for essential transition metals, pterin is unique in displaying multi-electron redox reactivity, an ability that resembles the redox capabilities of transition metals. It is perhaps because these two partners, metal and pterin,...
Transferrin is the serum iron transport protein in a wide variety of species. Its normal function is to transport iron through the blood between sites of uptake, utilization and storage. The protein consists of two distinct lobes, each of which contains a high affinity metal binding site. This review describes the thermodynamics of metal binding at these two sites, including the unique requirement...
The effect of DNA or nucleotides on the photophysical properties of metal polypyridyl complexes (especially those of ruthenium, osmium, rhodium, rhenium and copper) is reviewed. On binding to DNA the excited states of certain complexes show reduced non-radiative decay and protection from oxygen or water, while in other cases the excited state is quenched because of electron transfer from the nucleobases...
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