Stabilization of higher-valent states of iron porphyrin by hydroxide and methoxide ligands: electrochemical generation of iron(IV)-oxo porphyrins.
An electrochemical study of hydroxide- and methoxide-ligated iron(III) tetraphenylporphyrins possessing ortho-phenyl substituents that block mu-oxo dimer formation has been carried out. Ligation by these strongly basic oxyanions promotes the formation of iron(IV)-oxo porphyrins upon one-electron oxidation. Further one-electron oxidation of the latter provides the iron(IV)-oxo porphyrin pi-cation radical. These results are discussed in terms of chemical model studies and the enzymatic intermediate compounds I and II of the peroxidases.
D002712:Chlorides; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism; D004563:Electrochemistry; D006878:Hydroxides; D007501:Iron; D008665:Metalloporphyrins; D000432:Methanol; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000378:metabolism; D011166:Porphyrins
D002712:Chlorides; D006878:Hydroxides; D008665:Metalloporphyrins; D011166:Porphyrins; C032547:iron tetraphenylporphyrin; D003577:Cytochrome P-450 Enzyme System; C031356:hydroxide ion; D007501:Iron; D010544:Peroxidases; D000432:Methanol