Influence of Primary Coordination Sphere on Anion Rebound Selectivity in Nonheme Fe Enzyme-Catalyzed C(sp <sup>3</sup> )–H Functionalization: A Comparative Experimental and Computational Study of EgtB and ACCO
> OH > F. Furthermore, multivariate linear regression analysis revealed that fluorine atom abstraction is primarily governed by the intrinsic Fe-F bond strength, whereas fluorine rebound is predominantly controlled by the electronic structure of the Fe(III) intermediate. Together, these findings provide mechanistic insights into nonheme Fe enzymology and reprogramming toward selective radical rebound reactions, including challenging C-H fluorination.
Authors
- Peng Liu (ORCID: https://orcid.org/0000-0002-8188-632X)
- Binh Khanh (ORCID: https://orcid.org/0000-0001-8487-1417)
- Heyu Chen (ORCID: https://orcid.org/0000-0002-6068-9386)
- Yang Yang (ORCID: https://orcid.org/0000-0002-4956-2034)
- Rui Guo (ORCID: https://orcid.org/0000-0002-7436-8436)
- Liu-Peng Zhao (ORCID: https://orcid.org/0009-0000-5239-8135)
Institutions
- Howard Hughes Medical Institute (US)
- University of California, Santa Barbara (US)
- University of Pittsburgh (US)
Publication Details
- Journal
- Journal of the American Chemical Society
- Published
- 2026-07-17
- DOI
- https://doi.org/10.1021/jacs.6c06323
- Primary Topic
- Metal-Catalyzed Oxygenation Mechanisms
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- National Science Foundation
- David and Lucile Packard Foundation
- Howard Hughes Medical Institute
- Alfred P. Sloan Foundation
- Camille and Henry Dreyfus Foundation
- National Institutes of Health