Abstract
Abstract As the role of transition metal ions in biological systems becomes better understood, it has become apparent that various biological ligands strongly modulate the oxidation-reduction behavior of metal ions. Less well studied but no less important are the effects exerted by transition metal ions on the redox behavior of biologically important molecules, particularly those which normally function as electron transfer agents. Striking examples of this have been shown for a series of MgII and ZnII porphyrin complexes in which substitution of the metal ion for two protons sufficiently lowers the oxidation potential of the porphyrin so that it becomes fairly oxidizable in two successive 1e steps.1 Sirohemes in nitrite and sulfite reductases catalyze a remarkable 6e reduction in which the reducing ability of both the iron and the isobacteriochlorin are important.2,3 Metal ions are particularly important in modifying the redox behavior of substrates which coordinate in the active sites of metalloenzymes....
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