Research output: Chapter in Book/Report/Conference proceeding › Conference contribution › Research › peer-review
DFT predictions for hydrogen atom transfer at the [FeO]2+ group : A distinct activity of the oxyl state FeIII-O•. / Zilberberg, I. L.; Shubin, A. A.; Ruzankin, S. Ph et al.
International Conference of Computational Methods in Sciences and Engineering 2016, ICCMSE 2016. ed. / Zacharoula Kalogiratou; Theodore E. Simos; Theodore Monovasilis; Theodore E. Simos; Theodore E. Simos. American Institute of Physics Inc., 2016. 020027 (AIP Conference Proceedings; Vol. 1790).Research output: Chapter in Book/Report/Conference proceeding › Conference contribution › Research › peer-review
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TY - GEN
T1 - DFT predictions for hydrogen atom transfer at the [FeO]2+ group
T2 - International Conference of Computational Methods in Sciences and Engineering 2016, ICCMSE 2016
AU - Zilberberg, I. L.
AU - Shubin, A. A.
AU - Ruzankin, S. Ph
AU - Kovalskii, V. Yu
AU - Ovchinnikov, D. A.
AU - Parmon, V. N.
PY - 2016/12/6
Y1 - 2016/12/6
N2 - Iron (hydr)oxo complexes are becoming major subject of investigations in the field of hydrocarbon partial oxidation for industrial applications. Most challenging goal is to design the oxidation of methane to methanol as effective as the natural one-step process realized by methane monooxygenase under mild conditions. Key intermediate of iron enzymes is commonly agreed to be the complex containing the [FeO]2+ group. One may suggest that the same group on iron hydroxides would perform the same or higher reactivity toward the H-abstraction as that in enzymes. This suggestion was proved to be true by the presented DFT predictions on the methane hydrogen abstraction process at terminal Fe-oxo group in model mono-, di- and tetramer iron hydroxide clusters. The most important result obtained is a distinct activity of the radicaloid oxyl state FeIII-O• as compared to ferryl state FeIV=O for the same [FeO]2+ group. If the oxyl state is ground for terminal Fe-oxo group in hydroxides, then it is more active than the same group in mono-iron enzymes complexes. Since the electron configuration of the [FeO]2+ group in various ligand environment is always a mixture of oxyl and ferryl contributions, the activity of the [FeO]2+ group is determined by the oxyl contribution.
AB - Iron (hydr)oxo complexes are becoming major subject of investigations in the field of hydrocarbon partial oxidation for industrial applications. Most challenging goal is to design the oxidation of methane to methanol as effective as the natural one-step process realized by methane monooxygenase under mild conditions. Key intermediate of iron enzymes is commonly agreed to be the complex containing the [FeO]2+ group. One may suggest that the same group on iron hydroxides would perform the same or higher reactivity toward the H-abstraction as that in enzymes. This suggestion was proved to be true by the presented DFT predictions on the methane hydrogen abstraction process at terminal Fe-oxo group in model mono-, di- and tetramer iron hydroxide clusters. The most important result obtained is a distinct activity of the radicaloid oxyl state FeIII-O• as compared to ferryl state FeIV=O for the same [FeO]2+ group. If the oxyl state is ground for terminal Fe-oxo group in hydroxides, then it is more active than the same group in mono-iron enzymes complexes. Since the electron configuration of the [FeO]2+ group in various ligand environment is always a mixture of oxyl and ferryl contributions, the activity of the [FeO]2+ group is determined by the oxyl contribution.
KW - DFT
KW - ferryl
KW - H-abstraction barrier
KW - iron hydroxide
KW - methane
KW - oxyl
UR - http://www.scopus.com/inward/record.url?scp=85008600429&partnerID=8YFLogxK
U2 - 10.1063/1.4968653
DO - 10.1063/1.4968653
M3 - Conference contribution
AN - SCOPUS:85008600429
T3 - AIP Conference Proceedings
BT - International Conference of Computational Methods in Sciences and Engineering 2016, ICCMSE 2016
A2 - Kalogiratou, Zacharoula
A2 - Simos, Theodore E.
A2 - Monovasilis, Theodore
A2 - Simos, Theodore E.
A2 - Simos, Theodore E.
PB - American Institute of Physics Inc.
Y2 - 17 March 2016 through 20 March 2016
ER -
ID: 25403528