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Electrostatic and proton-electron interaction in membrane-bound charge transfer proteins under external electric

Zeinab Rahimi1,2, Amir Lohrasebi1, Thorsten Koslowski2

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Summary

The NrfH protein remains stable in electric fields, showing localized voltage changes and minor protonation shifts. This suggests its potential use in nanoscale bioelectronic devices.

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Area of Science:

  • Biophysics
  • Bioenergetics
  • Computational Biology

Background:

  • Membrane-bound charge transfer proteins are crucial for biological energy conversion and redox processes.
  • Their behavior under external electric fields is largely unknown, limiting applications in bio-nanoelectronics.

Purpose of the Study:

  • Investigate the response of the NrfH subunit from *Desulfovibrio vulgaris* to static electric fields.
  • Assess its potential for integration into bio-nanoelectronic devices.

Main Methods:

  • Employed a multiscale computational framework.
  • Utilized classical molecular dynamics with constant pH sampling.
  • Applied continuum dielectric theory and Laplace/Poisson solvers.

Main Results:

  • NrfH maintains structural integrity up to ±100 mV nm⁻¹.
  • Voltage drop is localized within the membrane or protein interior.
  • External fields induce pKa shifts, but only specific residues change protonation state.
  • Electron-proton coupling is weak, with energies generally smaller than kBT.

Conclusions:

  • NrfH exhibits significant electrostatic resilience.
  • The protein's properties suggest its utility as an electron-conducting element in nanoscale bioelectronic platforms.