Manganese substituted Compound I of cytochrome P450 biomimetics: a comparative reactivity study of Mn(V)-oxo versus Mn(IV)-oxo species.

Abstract:

:Manganese-oxo porphyrins have been well studied as biomimetic models of cytochromes P450 and are known to be able to catalyze substrate hydroxylation reactions. Recent experimental studies [J.Y. Lee, Y.-M. Lee, H. Kotani, W. Nam, S. Fukuzumi, Chem. Commun. (2009) 704] showed that Mn(V)-oxo porphyrins react rapidly with 10-methyl-9,10-dihydroacridine (AcrH(2)) via a proton-coupled-electron-transfer followed by an electron transfer. In this work, we present a computational study on the reactivity patterns of Mn(V)-oxo and Mn(IV)-oxo with respect to AcrH(2). This study shows that although both oxidants are capable of hydroxylating AcrH(2), the Mn(V)-oxo species is the more active oxidant. We have generalized these observations with thermodynamic cycles that explain the reaction mechanisms and electron transfer processes. For the Mn(V)-oxo mechanism the reactions proceed with a fast spin state crossing from the ground state singlet to the triplet spin state prior to a hydrogen atom transfer followed by another electron transfer. The present results are fully consistent with previous studies on iron-oxo porphyrins and manganese-oxo porphyrins and shows that the interplay of low lying singlet and triplet spin state surfaces influences the reaction mechanisms and kinetics.

journal_name

Arch Biochem Biophys

authors

Latifi R,Tahsini L,Karamzadeh B,Safari N,Nam W,de Visser SP

doi

10.1016/j.abb.2010.12.035

subject

Has Abstract

pub_date

2011-03-01 00:00:00

pages

4-13

issue

1

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(11)00003-8

journal_volume

507

pub_type

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