Probing the Effect of Mutations on Light Harvesting in CP29 by Transient Absorption and First-Principles Simulations

J Phys Chem Lett. 2024 Jun 20;15(24):6398-6408. doi: 10.1021/acs.jpclett.4c01040. Epub 2024 Jun 11.

Abstract

Natural light harvesting is exceptionally efficient thanks to the local energy funnel created within light-harvesting complexes (LHCs). To understand the design principles underlying energy transport in LHCs, ultrafast spectroscopy is often complemented by mutational studies that introduce perturbations into the excitonic structure of the natural complexes. However, such studies may fall short of identifying all excitation energy transfer (EET) pathways and their changes upon mutation. Here, we show that a synergistic combination of first-principles calculations and ultrafast spectroscopy can give unprecedented insight into the EET pathways occurring within LHCs. We measured the transient absorption spectra of the minor CP29 complex of plants and of two mutants, systematically mapping the kinetic components seen in experiments to the simulated exciton dynamics. With our combined strategy, we show that EET in CP29 is surprisingly robust to the changes in the exciton states induced by mutations, explaining the versatility of plant LHCs.

MeSH terms

  • Arabidopsis / chemistry
  • Arabidopsis / genetics
  • Arabidopsis / metabolism
  • Energy Transfer*
  • Kinetics
  • Light-Harvesting Protein Complexes* / chemistry
  • Light-Harvesting Protein Complexes* / genetics
  • Light-Harvesting Protein Complexes* / metabolism
  • Mutation*
  • Photosystem II Protein Complex

Substances

  • Light-Harvesting Protein Complexes
  • CP29 light harvesting complex
  • Photosystem II Protein Complex