View : 13 Download: 0

Manganese substituted Compound i of cytochrome P450 biomimetics: A comparative reactivity study of MnV-oxo versus MnIV-oxo species

Title
Manganese substituted Compound i of cytochrome P450 biomimetics: A comparative reactivity study of MnV-oxo versus MnIV-oxo species
Authors
Latifi R.Tahsini L.Karamzadeh B.Safari N.Nam W.De Visser S.P.
Ewha Authors
남원우
SCOPUS Author ID
남원우scopus
Issue Date
2011
Journal Title
Archives of Biochemistry and Biophysics
ISSN
0003-9861JCR Link
Citation
vol. 507, no. 1, pp. 4 - 13
Indexed
SCI; SCIE; SCOPUS WOS scopus
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 (AcrH2) 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 AcrH2. This study shows that although both oxidants are capable of hydroxylating AcrH2, the MnV-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 MnV-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. © 2010 Elsevier Inc. All rights reserved.
DOI
10.1016/j.abb.2010.12.035
Appears in Collections:
자연과학대학 > 화학·나노과학전공 > Journal papers
Files in This Item:
There are no files associated with this item.
Export
RIS (EndNote)
XLS (Excel)
XML


qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE