A Synthetic Model of Enzymatic [Fe₄S₄]–Alkyl Intermediates
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jacs.9b06975.pdf
Description
Published version
Size
977.02 KB
Format
Adobe PDF
Checksum (MD5)
f204534cec8c45702354a95c30e0957f
Author(s)
Ye, Mengshan
Thompson, Niklas B.
Brown, Alexandra C.
Suess, Daniel L. M.
Date Issued
August 2019
Journal
Journal of the American Chemical Society
Publisher
American Chemical Society (ACS)
Citation
Ye, Mengshan et al. "A Synthetic Model of Enzymatic [Fe₄S₄]–Alkyl Intermediates." Journal of the American Chemical Society 141, 34 (August 2019): 13330-13335 © 2019 American Chemical Society
Version
Final published version
Abstract
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+, Mössbauer 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.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
Terms of Use
Creative Commons Attribution-NonCommercial-NoDerivs License
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DOI of Published Version
https://doi.org/10.1021/jacs.9b06975
