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Iron-sulfur clusters: the road to room temperature

Author(s)
Skeel, Brighton A.; Suess, Daniel L. M.
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Abstract
Iron-sulfur proteins perform a wide variety of reactions central to the metabolisms of all living organisms. Foundational to their reaction chemistry are the rich electronic structures of their constituent Fe-S clusters, which differ in important ways from the active sites of mononuclear Fe enzymes. In this perspective, we summarize the essential electronic structure features that make Fe-S clusters unique, and point to the need for studies aimed at understanding the electronic basis for their reactivity under physiological conditions. Specifically, at ambient temperature, both the ground state and a large number of excited states are thermally populated, and thus a complete understanding of Fe-S cluster reactivity must take into account the properties, energies, and reactivity patterns of these excited states. We highlight prior research toward characterizing the low-energy excited states of Fe-S clusters that has established what is now a consensus model of these excited state manifolds and the bonding interactions that give rise to them. In particular, we discuss the low-energy alternate spin states and valence electron configurations that occur in Fe-S clusters of varying nuclearities, and finally suggest that there may be unrecognized functional roles for these states. Graphical abstract
Date issued
2025-01-31
URI
https://hdl.handle.net/1721.1/158250
Department
Massachusetts Institute of Technology. Department of Chemistry
Journal
Journal of Biological Inorganic Chemistry
Publisher
Springer International Publishing
Citation
Skeel, B.A., Suess, D.L.M. Iron-sulfur clusters: the road to room temperature. J Biol Inorg Chem (2025).
Version: Final published version

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