{
  "abstract": "Most enzymatic systems that couple ATP hydrolysis to low-potential electron transfer (ET) typically rely on: (i) large conformational changes that tune the redox properties of the reductase Fe-S cluster, and (ii) redox state-dependent dissociation of the reductase subunit to ensure directionality. The double-cubane cluster protein (DCCP) and its reductase (DCCP-R) operate through a distinct mechanism, as the complex remains associated and the crystal structures reveal only subtle nucleotide-dependent conformational changes. These include the formation of Asp–Arg salt bridges by two aspartates (Asp113), located next to the [4Fe4S] cluster at the DCCP:DCCP-R interface. Infrared spectroscopy further showed that protein scaffold rearrangements are rate-limiting and likely involve carboxylate protonation dynamics. In addition, direct electrochemistry revealed an unusually high midpoint potential for a low-potential [4Fe4S] cluster. DFT modeling demonstrated that the ATP-dependent conformational change is coupled to the protonation status of Asp113 in proximity to the [4Fe4S] electron relay. This coupling modulates the cluster redox behavior in an electrostatic proton-coupled ET (PCET) manner, providing a thermodynamic basis for electron transfer to the low-potential [8Fe9S] cluster in DCCP.",
  "abstract_shown": true,
  "affiliations": [
    "Institut für Chemie",
    "Technische Universität Berlin",
    "Instituto de Química Física de los Materiales, Medio Ambiente y Energía / Departamento de Química Inorgánica, Analítica y Química Física, Facultad de Ciencias Exactas y Naturales",
    "Universidad de Buenos Aires (UBA) / CONICET",
    "School of Chemistry",
    "University College Dublin Belfield",
    "Institut für Biologie",
    "Humboldt-Universität zu Berlin"
  ],
  "article_type": null,
  "arxiv": null,
  "author_total": 9,
  "authors": [
    {
      "affs": [
        0,
        1,
        2,
        3
      ],
      "name": "Ulises A. Zitare",
      "orcid": "0000-0003-0248-6916"
    },
    {
      "affs": [
        0,
        1
      ],
      "name": "Vladimir Pelmenschikov",
      "orcid": "0000-0002-0523-4418"
    },
    {
      "affs": [
        0,
        1
      ],
      "name": "Sagie Katz",
      "orcid": "0000-0001-8526-183X"
    },
    {
      "affs": [
        0,
        1
      ],
      "name": "Zishuo Zhang"
    },
    {
      "affs": [
        0,
        1,
        4,
        5
      ],
      "name": "Nadia Elghobashi-Meinhardt",
      "orcid": "0000-0002-1023-6856"
    },
    {
      "affs": [
        6,
        7
      ],
      "name": "Jae-Hun Jeoung",
      "orcid": "0000-0003-0546-8342"
    },
    {
      "affs": [
        6,
        7
      ],
      "name": "Holger Dobbek",
      "orcid": "0000-0002-4122-3898"
    },
    {
      "affs": [
        0,
        1
      ],
      "name": "Maria Andrea Mroginski",
      "orcid": "0000-0002-7497-5631"
    },
    {
      "affs": [
        0,
        1
      ],
      "name": "Ingo Zebger",
      "orcid": "0000-0002-6354-3585"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/26cp3qm85pc0r.bib",
  "cited_by": 0,
  "doi": "10.26434/chemrxiv.15009538/v1",
  "fulltext_url": null,
  "id": "26cp3qm85pc0r",
  "issns": [],
  "landing_url": "https://chemrxiv.org/doi/full/10.26434/chemrxiv.15009538/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": "W7214600015",
  "pdf_url": "https://chemrxiv.org/doi/pdf/10.26434/chemrxiv.15009538/v1",
  "pmcid": null,
  "pmid": null,
  "published": "2026-09-28",
  "publisher": "American Chemical Society (ACS)",
  "ris": "https://research.draconitic.com/paper/26cp3qm85pc0r.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:17:21Z",
      "native_id": "10.26434/chemrxiv.15009538",
      "source": "chemrxiv",
      "url": "https://chemrxiv.org/doi/full/10.26434/chemrxiv.15009538/v1"
    }
  ],
  "subjects": [
    {
      "field": "chemistry",
      "origin": "source:chemrxiv",
      "subfield": "general"
    }
  ],
  "title": "ATP-Driven Electron Transfer in the DCCP:DCCP-R Protein: A Synergy of Conformational Shift and Asp–Arg Bridge Protonation for Redox Modulation",
  "title_text": "ATP-Driven Electron Transfer in the DCCP:DCCP-R Protein: A Synergy of Conformational Shift and Asp–Arg Bridge Protonation for Redox Modulation",
  "type": "preprint",
  "updated_at": "2026-10-30T12:17:21Z",
  "url": "https://research.draconitic.com/paper/26cp3qm85pc0r",
  "venue": "ChemRxiv",
  "versions": []
}