Simulating Redox Potentials of Biomolecules: the Case of Cryptochrome 1 from Arabidopsis thaliana

11 February 2019, Version 1
This content is a preprint and has not undergone peer review at the time of posting.


Redox reactions play a key role in various biological processes, including photosynthesis and respiration. Quantitative and predictive computational characterization of redox events is therefore highly desirable for enriching our knowledge on mechanistic features of biological redox-active macromolecules. Here, we present the results of computational studies of the redox potential of flavin adenine dinucleotide (FAD) in cryptochrome 1 from Arabidopsis thaliana (Cry1At). The special attention is paid to fundamental aspects of the theoretical description such as the effects of environment polarization and of the long-range electrostatic interactions on the computed energetic parameters. Environment (protein and the solvent) polarization is shown to be crucial for accurate estimates of the redox potential: hybrid quantum-classical results with and without account for environment polarization differ by 1.4 V. Long-range electrostatic interactions are shown to contribute significantly to the computed redox potential value even at the distances far beyond the protein outer surface. The theoretical estimate (0.07 V) of the midpoint reduction potential of FAD in Cry1At is reported for the first time and is in good agreement with available experimental data.


redox potential
density functional theory
polarizable force field
effective fragment potential
Poisson-Boltzmann equation

Supplementary materials

supporting information


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