{
  "abstract": "Nature readily employs iron–sulfur (Fe–S) clusters to perform a wide range of essential biological processes involving long-range electron transport and catalysis for kinetically challenging redox chemistry. Notably, the structure of Fe–S cubane ([Fe4S4]) metalloclusters that serve as electron transfer mediators are highly conserved, where ligand coordination to four cysteine residues anchors the cofactor within metalloproteins such as ferredoxins (Fds) and high-potential iron-sulfur protein (HiPIPs). Despite sharing the same primary coordination environment, the [Fe4S4] cofactors within Fds and HiPIPs operate with discrete redox couples and potential windows that afford distinct electrochemical properties depending on the Fe–S secondary coordination sphere and protein environment. This enables [Fe4S4] clusters to serve as versatile coupling partners for kinetically challenging redox reactions spanning the full range of biologically accessible reduction potentials. The electrochemical properties of [Fe4S4] clusters are tuned through the cooperative interplay between its strongly-correlated electronic structure and the noncovalent interactions within its secondary-sphere and protein environments. Significant experimental and computational efforts have been made to identify the structure-function relationships driving selective modulation of cluster electrochemical features; however, disentangling this complex interplay remains a significant challenge. Here, we employ a low-scaling, multi-reference computational approach to elucidate how secondary-sphere interactions, namely hydrogen bonding (H-bonding) and solvent electrostatics, tune the electronic structure of biomimetic [Fe4S4] clusters and give rise to the diverging redox properties observed across different protein scaffolds in biological systems.",
  "abstract_shown": true,
  "affiliations": [],
  "article_type": null,
  "arxiv": null,
  "author_total": 2,
  "authors": [
    {
      "name": "Shelby T. Davis"
    },
    {
      "name": "Jan-Niklas Boyn",
      "orcid": "0000-0002-6240-3759"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/aqbybfjc94ddw.bib",
  "cited_by": 0,
  "doi": "10.26434/chemrxiv.15008641/v1",
  "fulltext_url": null,
  "id": "aqbybfjc94ddw",
  "issns": [],
  "landing_url": "https://chemrxiv.org/doi/full/10.26434/chemrxiv.15008641/v1",
  "language": null,
  "licence": "CC-BY-NC-ND",
  "licence_label": "CC BY-NC-ND",
  "licence_source": "journal",
  "licence_url": "https://creativecommons.org/licenses/by-nc-nd/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "openalex",
      "2105|Metalloenzymes and iron-sulfur proteins"
    ]
  ],
  "openalex": "W7212176616",
  "pdf_url": "https://chemrxiv.org/doi/pdf/10.26434/chemrxiv.15008641/v1",
  "pmcid": null,
  "pmid": null,
  "published": "2026-09-10",
  "publisher": "American Chemical Society (ACS)",
  "ris": "https://research.draconitic.com/paper/aqbybfjc94ddw.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:17:19Z",
      "native_id": "10.26434/chemrxiv.15008641",
      "source": "chemrxiv",
      "url": "https://chemrxiv.org/doi/full/10.26434/chemrxiv.15008641/v1"
    }
  ],
  "subjects": [
    {
      "field": "chemistry",
      "origin": "source:chemrxiv",
      "subfield": "general"
    }
  ],
  "title": "Elucidating Secondary Coordination Sphere Effects on the Electronic Structure and Redox Properties of Biomimetic Iron–Sulfur Cubanes",
  "title_text": "Elucidating Secondary Coordination Sphere Effects on the Electronic Structure and Redox Properties of Biomimetic Iron–Sulfur Cubanes",
  "type": "preprint",
  "updated_at": "2026-10-30T12:17:19Z",
  "url": "https://research.draconitic.com/paper/aqbybfjc94ddw",
  "venue": "ChemRxiv",
  "versions": []
}