A Synthetic Model of Enzymatic [Fe4S4]–Alkyl Intermediates
| Autor: | Niklas B. Thompson, Alexandra C. Brown, Daniel L. M. Suess, Mengshan Ye |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
chemistry.chemical_classification
Valence (chemistry) Charge density General Chemistry 010402 general chemistry 01 natural sciences Biochemistry Catalysis 0104 chemical sciences Enzyme catalysis Crystallography chemistry.chemical_compound Delocalized electron Colloid and Surface Chemistry chemistry Cubane Mössbauer spectroscopy Cluster (physics) Alkyl |
| Zdroj: | Journal of the American Chemical Society. 141:13330-13335 |
| ISSN: | 1520-5126 0002-7863 |
| DOI: | 10.1021/jacs.9b06975 |
| Popis: | Although alkyl complexes of [Fe4S4] clusters have been invoked as intermediates in a number of enzymatic reactions, obtaining a detailed understanding of their reactivity patterns and electronic structures has been difficult owing to their transient nature. To address this challenge, we herein report the synthesis and characterization of a 3:1 site-differentiated [Fe4S4]2+–alkyl cluster. Whereas [Fe4S4]2+ clusters typically exhibit pairwise delocalized electronic structures in which each Fe has a formal valence of 2.5+, Mossbauer spectroscopic and computational studies suggest that the highly electron-releasing alkyl group partially localizes the charge distribution within the cubane, an effect that has not been previously observed in tetrahedrally coordinated [Fe4S4] clusters. |
| Databáze: | OpenAIRE |
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