Mechanism of catalyst activation in iron(porphyrin)-catalysed aerobic oxidative cleavage of 2,3-dimethylindole
Ferric porphyrins catalyse the aerobic oxidative cleavage of 2,3-dimethylindole, mimicking dioxygenase enzymes. The data herein suggest that the indole reduces the Fe<sup>III</sup>(porphyrin) to Fe<sup>II</sup>(porphyrin) <i>via</i> a proton-coupled electron transfer mechanism. Subsequently, Fe<sup>II</sup>(porphyrin) binds O<sub>2</sub> and generates the critical superoxo intermediate, which oxidatively cleaves a second equivalent of substrate.
Authors
- Seth Olsen (ORCID: https://orcid.org/0000-0002-3822-753X)
- Anna C. Brezny (ORCID: https://orcid.org/0000-0002-3002-1828)
- James H. Lyke
- Emma R. Straton
- Olha Zubarieva
Institutions
- Skidmore College (US)
- St. Olaf College (US)
Publication Details
- Journal
- Dalton Transactions
- Published
- 2025-01-01
- DOI
- https://doi.org/10.1039/d5dt01271f
- Primary Topic
- Metal-Catalyzed Oxygenation Mechanisms
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- Skidmore College
- St. Olaf College
- American Chemical Society Petroleum Research Fund