Iron oxidation titation lab backcalculation
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The adjacent sites of the coordination sphere are solvated until cofactor and substrates bind.Ī subfamily of oxygenases containing the 2-His-1-carboxylate motif are the α-ketoglutarate (αKG)-dependent enzymes. Representation of the 2-His-1-carboxylate facial triad, where the histidine and carboxylate side chains are bound to one face of the iron. In the dioxygenase family of enzymes, the 2-His-1-carboxylate facial triad affords proximity of the substrate(s) and dioxygen to ensure efficient catalysis of reactions such as the repair of alkylated DNA/RNA, the biosynthesis of penicillin, and the degradation of aromatic compounds for carbon sequestration. 4, 5 This metal binding configuration involves the side-chains of two histidine and one aspartate/glutamate amino acid residues to occupy one face of the Fe 2+ octahedral coordination sphere, leaving the adjacent face coordinated to solvent ligands which are easily exchanged for binding substrates ( Figure 1). A common motif found in a range of non-heme Fe 2+ oxygenases is the 2-His-1-carboxylate facial triad.
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1– 3 Many complexes of Fe 2+ spontaneously react with dioxygen to generate high-valent intermediates which are fundamental for the biological and environmental processes they catalyze. Mononuclear Fe 2+ sites can be found throughout nature at the catalytic centers of many important enzymes.