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PreprintCC BY-NC-NDChemRxiv

ATP-Driven Electron Transfer in the DCCP:DCCP-R Protein: A Synergy of Conformational Shift and Asp–Arg Bridge Protonation for Redox Modulation

  • Ulises A. Zitare1,2,3,4
  • Vladimir Pelmenschikov1,2
  • Sagie Katz1,2
  • Zishuo Zhang1,2
  • Nadia Elghobashi-Meinhardt1,2,5,6
  • Jae-Hun Jeoung7,8
  • Holger Dobbek7,8
  • Maria Andrea Mroginski1,2
  • Ingo Zebger1,2
8 affiliations
  1. 1Institut für Chemie
  2. 2Technische Universität Berlin
  3. 3Instituto de Química Física de los Materiales, Medio Ambiente y Energía / Departamento de Química Inorgánica, Analítica y Química Física, Facultad de Ciencias Exactas y Naturales
  4. 4Universidad de Buenos Aires (UBA) / CONICET
  5. 5School of Chemistry
  6. 6University College Dublin Belfield
  7. 7Institut für Biologie
  8. 8Humboldt-Universität zu Berlin
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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.

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Cite

BibTeXRIS
BibTeX
@misc{zitare2026atpdriven,
  title = {{ATP-Driven Electron Transfer in the DCCP:DCCP-R Protein: A Synergy of Conformational Shift and Asp–Arg Bridge Protonation for Redox Modulation}},
  author = {Ulises A. Zitare and Vladimir Pelmenschikov and Sagie Katz and Zishuo Zhang and Nadia Elghobashi-Meinhardt and Jae-Hun Jeoung and Holger Dobbek and Maria Andrea Mroginski and Ingo Zebger},
  howpublished = {ChemRxiv},
  year = {2026},
  month = sep,
  doi = {10.26434/chemrxiv.15009538/v1},
  url = {https://chemrxiv.org/doi/full/10.26434/chemrxiv.15009538/v1},
  note = {CC BY-NC-ND},
}
RIS
TY  - UNPB
TI  - ATP-Driven Electron Transfer in the DCCP:DCCP-R Protein: A Synergy of Conformational Shift and Asp–Arg Bridge Protonation for Redox Modulation
AU  - Ulises A. Zitare
AU  - Vladimir Pelmenschikov
AU  - Sagie Katz
AU  - Zishuo Zhang
AU  - Nadia Elghobashi-Meinhardt
AU  - Jae-Hun Jeoung
AU  - Holger Dobbek
AU  - Maria Andrea Mroginski
AU  - Ingo Zebger
PY  - 2026
DA  - 2026/09/28
PB  - ChemRxiv
DO  - 10.26434/chemrxiv.15009538/v1
UR  - https://chemrxiv.org/doi/full/10.26434/chemrxiv.15009538/v1
AB  - 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.
ER  -