Full metadata record
DC Field | Value | Language |
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dc.contributor.author | 남원우 | * |
dc.date.accessioned | 2016-08-28T12:08:19Z | - |
dc.date.available | 2016-08-28T12:08:19Z | - |
dc.date.issued | 2011 | * |
dc.identifier.issn | 0003-9861 | * |
dc.identifier.other | OAK-7358 | * |
dc.identifier.uri | https://dspace.ewha.ac.kr/handle/2015.oak/221433 | - |
dc.description.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. | * |
dc.language | English | * |
dc.title | Manganese substituted Compound i of cytochrome P450 biomimetics: A comparative reactivity study of MnV-oxo versus MnIV-oxo species | * |
dc.type | Article | * |
dc.relation.issue | 1 | * |
dc.relation.volume | 507 | * |
dc.relation.index | SCI | * |
dc.relation.index | SCIE | * |
dc.relation.index | SCOPUS | * |
dc.relation.startpage | 4 | * |
dc.relation.lastpage | 13 | * |
dc.relation.journaltitle | Archives of Biochemistry and Biophysics | * |
dc.identifier.doi | 10.1016/j.abb.2010.12.035 | * |
dc.identifier.wosid | WOS:000287722700003 | * |
dc.identifier.scopusid | 2-s2.0-79951559118 | * |
dc.author.google | Latifi R. | * |
dc.author.google | Tahsini L. | * |
dc.author.google | Karamzadeh B. | * |
dc.author.google | Safari N. | * |
dc.author.google | Nam W. | * |
dc.author.google | De Visser S.P. | * |
dc.contributor.scopusid | 남원우(7006569723) | * |
dc.date.modifydate | 20240116111857 | * |