dc.contributor.author | Opalade, Adedamola A. | |
dc.contributor.author | Grotemeyer, Elizabeth N. | |
dc.contributor.author | Jackson, Timothy A. | |
dc.date.accessioned | 2022-02-09T16:28:52Z | |
dc.date.available | 2022-02-09T16:28:52Z | |
dc.date.issued | 2021-11-25 | |
dc.identifier.citation | Opalade, A.A.; Grotemeyer, E.N.; Jackson, T.A. Mimicking Elementary Reactions of Manganese Lipoxygenase Using Mn-hydroxo and Mn-alkylperoxo Complexes. Molecules 2021, 26, 7151. https://doi.org/10.3390/molecules26237151 | en_US |
dc.identifier.uri | http://hdl.handle.net/1808/32517 | |
dc.description.abstract | Manganese lipoxygenase (MnLOX) is an enzyme that converts polyunsaturated fatty acids to alkyl hydroperoxides. In proposed mechanisms for this enzyme, the transfer of a hydrogen atom from a substrate C-H bond to an active-site MnIII-hydroxo center initiates substrate oxidation. In some proposed mechanisms, the active-site MnIII-hydroxo complex is regenerated by the reaction of a MnIII-alkylperoxo intermediate with water by a ligand substitution reaction. In a recent study, we described a pair of MnIII-hydroxo and MnIII-alkylperoxo complexes supported by the same amide-containing pentadentate ligand (6Medpaq). In this present work, we describe the reaction of the MnIII-hydroxo unit in C-H and O-H bond oxidation processes, thus mimicking one of the elementary reactions of the MnLOX enzyme. An analysis of kinetic data shows that the MnIII-hydroxo complex [MnIII(OH)(6Medpaq)]+ oxidizes TEMPOH (2,2′-6,6′-tetramethylpiperidine-1-ol) faster than the majority of previously reported MnIII-hydroxo complexes. Using a combination of cyclic voltammetry and electronic structure computations, we demonstrate that the weak MnIII-N(pyridine) bonds lead to a higher MnIII/II reduction potential, increasing the driving force for substrate oxidation reactions and accounting for the faster reaction rate. In addition, we demonstrate that the MnIII-alkylperoxo complex [MnIII(OOtBu)(6Medpaq)]+ reacts with water to obtain the corresponding MnIII-hydroxo species, thus mimicking the ligand substitution step proposed for MnLOX. | en_US |
dc.publisher | MDPI | en_US |
dc.rights | © 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license. | en_US |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | en_US |
dc.subject | Manganese enzymes | en_US |
dc.subject | Lipoxygenase | en_US |
dc.subject | Hydrogen-atom transfer | en_US |
dc.subject | Ligand substitution | en_US |
dc.subject | Alkylperoxo | en_US |
dc.title | Mimicking Elementary Reactions of Manganese Lipoxygenase Using Mn-hydroxo and Mn-alkylperoxo Complexes | en_US |
dc.type | Article | en_US |
kusw.kuauthor | Opalade, Adedamola A. | |
kusw.kuauthor | Grotemeyer, Elizabeth N. | |
kusw.kuauthor | Jackson, Timothy A. | |
kusw.kudepartment | Chemistry | en_US |
kusw.kudepartment | Center for Environmentally Beneficial Catalysis | en_US |
dc.identifier.doi | 10.3390/molecules26237151 | en_US |
dc.identifier.orcid | https://orcid.org/ 0000-0002-3529-2715 | en_US |
kusw.oaversion | Scholarly/refereed, publisher version | en_US |
kusw.oapolicy | This item meets KU Open Access policy criteria. | en_US |
dc.identifier.pmid | PMC8659247 | en_US |
dc.rights.accessrights | openAccess | en_US |