Iron-sulfur clusters: the road to room temperature

Skeel, Brighton A.; Suess, Daniel L. M.

doi:10.1007/s00775-025-02094-0

Title: Iron-sulfur clusters: the road to room temperature

Journal Article · 31 January 2025 · JBIC Journal of Biological Inorganic Chemistry

DOI: https://doi.org/10.1007/s00775-025-02094-0 · OSTI ID:2536817

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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

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Sponsoring Organization:: USDOE

Grant/Contract Number:: SC0020974

OSTI ID:: 2536817

Journal Information:: JBIC Journal of Biological Inorganic Chemistry, Journal Name: JBIC Journal of Biological Inorganic Chemistry Journal Issue: 2 Vol. 30; ISSN 1432-1327

Publisher:: Springer Science + Business MediaCopyright Statement

Country of Publication:: Germany

Language:: English

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