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Bioexcitons by Design: How Do We Get There?

Mike Reppert
Published in: The journal of physical chemistry. B (2023)
Biological pigment-protein complexes (PPCs) exhibit a remarkable ability to tune the optical properties of biological excitons (bioexcitons) through specific pigment-protein interactions. While such fine-tuning allows natural systems (e.g., photosynthetic proteins) to carry out their native functions with near-optimal performance, native function itself is often suboptimal for applications such as biofuel production or quantum technology development. This perspective offers a look at near-term prospects for the rational reoptimization of PPC bioexcitons for new functions using site-directed mutagenesis. The primary focus is on the "structure-spectrum" challenge of understanding the relationships between structural features and spectroscopic properties. While recent examples demonstrate that site-directed mutagenesis can be used to tune nearly all key bioexciton parameters (e.g., site energies, interpigment couplings, and electronic-vibrational interactions), critical challenges remain before we achieve truly rational design of bioexciton properties.
Keyphrases
  • crispr cas
  • density functional theory
  • protein protein
  • amino acid
  • molecular dynamics
  • air pollution
  • molecular docking
  • preterm infants
  • energy transfer
  • binding protein
  • small molecule
  • preterm birth
  • monte carlo