| Autor: |
Field MJ; Department of Chemistry and Department of Molecular Biology and Biochemistry, University of California, Irvine, California92697, United States., Oyala PH; Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California91125, United States., Green MT; Department of Chemistry and Department of Molecular Biology and Biochemistry, University of California, Irvine, California92697, United States. |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of the American Chemical Society [J Am Chem Soc] 2022 Oct 26; Vol. 144 (42), pp. 19272-19283. Date of Electronic Publication: 2022 Oct 14. |
| DOI: |
10.1021/jacs.2c05459 |
| Abstrakt: |
Although the activation of inert C-H bonds by metal-oxo complexes has been widely studied, important questions remain, particularly regarding the role of oxygen spin population (i.e., unpaired electrons on the oxo ligand) in facilitating C-H bond cleavage. In order to shed light on this issue, we have utilized 17 O electron nuclear double resonance spectroscopy to measure the oxygen spin populations of three compound I intermediates in heme enzymes with different reactivities toward C-H bonds: chloroperoxidase, cytochrome P450, and a selenolate (selenocysteinyl)-ligated cytochrome P450. The experimental data suggest an inverse correlation between oxygen spin population and electron donation from the axial ligand. We have explored the implications of this result using a Hückel-type molecular orbital model and constrained density functional theory calculations. These investigations have allowed us to examine the relationship between oxygen spin population, oxygen charge, electron donation from the axial ligand, and reactivity. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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