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DC Field | Value | Language |
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dc.citation.endPage | 15996 | - |
dc.citation.number | 51 | - |
dc.citation.startPage | 15983 | - |
dc.citation.title | JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | - |
dc.citation.volume | 129 | - |
dc.contributor.author | Decker, Andrea | - |
dc.contributor.author | Rohde, Jan-Uwe | - |
dc.contributor.author | Klinker, Eric J. | - |
dc.contributor.author | Wong, Shaun D. | - |
dc.contributor.author | Que, Lawrence, Jr. | - |
dc.contributor.author | Solomon, Edward I. | - |
dc.date.accessioned | 2023-12-22T09:07:31Z | - |
dc.date.available | 2023-12-22T09:07:31Z | - |
dc.date.created | 2015-07-03 | - |
dc.date.issued | 2007-12 | - |
dc.description.abstract | High-valent Fe-IV=O species are key intermediates in the catalytic cycles of many mononuclear non-heme iron enzymes and have been structurally defined in model systems. Variable-temperature magnetic circular dichroism (VT-MCD) spectroscopy has been used to evaluate the electronic structures and in particular the Fe-O bonds of three Fe-IV=O (S = 1) model complexes, [Fe-IV(O)(TMC)(NCMe)](2+), [Fe-IV(O)(TMC)(OC(O)CF3)](+), and [Fe-IV(O)(N4py)](2+). These complexes are characterized by their strong and covalent Fe-O pi-bonds. The MCD spectra show a vibronic progression in the nonbonding -> pi(*) excited state, providing the Fe-O stretching frequency and the Fe-O bond length in this excited state and quantifying the pi-contribution to the total Fe-O bond. Correlation of these experimental data to reactivity shows that the [Fe-IV(O)(N4py)](2+) complex, with the highest reactivity toward hydrogen-atom abstraction among the three, has the strongest Fe-O pi-bond. Density functional calculations were correlated to the data and support the experimental analysis. The strength and covalency of the Fe-O pi-bond result in high oxygen character in the important frontier molecular orbitals (FMOs) for this reaction, the unoccupied beta-spin d(xz/yz) orbitals, that activates these for electrophilic attack. An extension to biologically relevant Fe-IV=O (S = 2) enzyme intermediates shows that these can perform electrophilic attack reactions along the same mechanistic pathway (pi-FMO pathway) with similar reactivity but also have an additional reaction channel involving the unoccupied alpha-spin d(z(2)) orbital (sigma-FMO pathway). These studies experimentally probe the FMOs involved in the reactivity of Fe-IV=O (S = 1) model complexes resulting in a detailed understanding of the Fe-O bond and its contributions to reactivity | - |
dc.identifier.bibliographicCitation | JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, v.129, no.51, pp.15983 - 15996 | - |
dc.identifier.doi | 10.1021/ja074900s | - |
dc.identifier.issn | 0002-7863 | - |
dc.identifier.scopusid | 2-s2.0-84962419519 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/11974 | - |
dc.identifier.url | http://pubs.acs.org/doi/abs/10.1021/ja074900s | - |
dc.identifier.wosid | 000251974000049 | - |
dc.language | 영어 | - |
dc.publisher | AMER CHEMICAL SOC | - |
dc.title | Spectroscopic and quantum chemical studies on low-spin Fe-IV=O complexes: Fe-O bonding and its contributions to reactivity | - |
dc.type | Article | - |
dc.description.isOpenAccess | FALSE | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordPlus | TAURINE/ALPHA-KETOGLUTARATE DIOXYGENASE | - |
dc.subject.keywordPlus | EFFECTIVE CORE POTENTIALS | - |
dc.subject.keywordPlus | NONHEME IRON ENZYMES | - |
dc.subject.keywordPlus | HYDROGEN-ATOM ABSTRACTION | - |
dc.subject.keywordPlus | ELECTRONIC-STRUCTURES | - |
dc.subject.keywordPlus | AB-INITIO | - |
dc.subject.keywordPlus | MOLECULAR CALCULATIONS | - |
dc.subject.keywordPlus | OXYGEN ACTIVATION | - |
dc.subject.keywordPlus | OXOIRON(IV) COMPLEX | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
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