Spectroscopic observation of iodosylarene metalloporphyrin adducts and manganese(V)-oxo porphyrin species in a cytochrome P450 analogue

Mian Guo, Hang Dong, Jie Li, Ben Cheng, Yun-qing Huang, Yu-qi Feng and Aiwen Lei ()
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Mian Guo: College of Chemistry and Molecular Sciences, Wuhan University
Hang Dong: College of Chemistry and Molecular Sciences, Wuhan University
Jie Li: College of Chemistry and Molecular Sciences, Wuhan University
Ben Cheng: College of Chemistry and Molecular Sciences, Wuhan University
Yun-qing Huang: Key Laboratory of Analytical Chemistry for Biology and Medicine (Ministry of Education), College of Chemistry and Molecular Sciences, Wuhan University
Yu-qi Feng: Key Laboratory of Analytical Chemistry for Biology and Medicine (Ministry of Education), College of Chemistry and Molecular Sciences, Wuhan University
Aiwen Lei: College of Chemistry and Molecular Sciences, Wuhan University

Nature Communications, 2012, vol. 3, issue 1, 1-9

Abstract: Abstract Different metalloporphyrin model compounds have been synthesized to study the mechanisms of cytochrome P450s with various terminal oxidants, and numerous intermediates have been reported. However, the detailed mechanism of the oxygen atom transfer from iodosylarene to the substrates remains unclear. Here we report the direct ultraviolet-visible spectroscopic observation of the soluble iodosylarene-manganese porphyrin adduct following catalytic oxidation using 2,4,6-tri-tert-butylphenol as the reductant. When the reductant is changed to cis-stilbene, the rate-determining step also changes. Both the iodosylarene-manganese porphyrin adduct and [(porphyrin)Mn(V)=O] species may be simultaneously observed. In the absence of reductant, the adduct of iodosylarene with sterically hindered [Mn(meso-tetrakis(2,6-dichlorophenyl)porphinato)Cl] is immediately formed, and smoothly converted into a high-valent [(porpyrinato)Mn=O]. Electrospray ionization mass spectrometry analysis of the reaction further confirms the transformation between these species. This study provides an insight into the mechanism of oxygen transfer within the haem-containing enzymatic systems.

Date: 2012
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DOI: 10.1038/ncomms2196

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