Abstract
Extensive research in the past decades has shown that nature relies on high-valent iron (IV,V) porphyrins in a number of enzyme-directed processes of heme proteins. For example, hydroxylation reaction catalyzed by cytochrome P450 involves an iron porphyrin intermediate which contains the oxoferryl moiety (Fe(IV)O). Liver microsomal cytochrome P450-LM 3,4 is known to catalyze the transfer of a functionalized nitrogen atom intra- as well as inter-molecularly, and the proposed reaction cycle presumably involves a high-valent iron porphyrin intermediate which contains the nitrido-iron moiety(Fe(V)N). This review is focused on the biological significance of these high-valent iron(IV,V) porphyrins and their Fe(IV)O and Fe(V)N stretching vibrations observed in resonance Raman spectra.
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