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DFT calculations were performed to rationalize the mechanism of reduction of these compounds. The three complexes undergo a two\u2010electron transfer whose the mechanism depends on the bulkiness of the dithiolate bridge, which involves a different timing of the structural changes (Fe\u2212S bond cleavage, inversion of conformation and CO bridging) vs redox steps. The introduction of a bulky group in the dithiolate linker has obviously an effect on normally ordered (as for propanedithiolate (pdt)) or inverted (pdt<jats:sup>Et2<\/jats:sup>, pdt<jats:sup>Bn2<\/jats:sup>) reduction potentials. Et\u2192Bn replacement is not theoretically predicted to alter the geometry and energy of the most stable mono\u2010reduced and bi\u2010reduced forms but such a replacement alters the kinetics of the electron transfer vs the structural changes.<\/jats:p>","DOI":"10.1002\/chem.202300569","type":"journal-article","created":{"date-parts":[[2023,4,4]],"date-time":"2023-04-04T22:20:36Z","timestamp":1680646836000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":12,"title":["Normal vs. Inverted Ordering of Reduction Potentials in [FeFe]\u2010Hydrogenases Biomimetics: Effect of the Dithiolate Bulk"],"prefix":"10.1002","volume":"29","author":[{"given":"Federica","family":"Arrigoni","sequence":"first","affiliation":[{"name":"Department of Biotechnology and Bioscience University of Milano-Bicocca  Piazza della Scienza 2 20126 Milan Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Luca","family":"De 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