Mechanistic Regimes of Vibronic Transport in a Heterodimer and the Design Principle of Incoherent Vibronic Transport in Phycobiliproteins

Following the observation of coherent oscillations in nonlinear spectra of photosynthetic pigment protein complexes, in particular, phycobilliproteins such as PC645, coherent vibronic transport has been suggested as a design principle for novel light-harvesting materials. Vibronic transport between energetically remote pigments is coherent when the presence of a vibration resonant with the electronic energy gap supports transient delocalization between the electronic excited states. We establish the mechanism of vibronic transport for a model heterodimer across a wide range of molecular parameter values. The resulting mechanistic map demonstrates that the molecular parameters of phycobiliproteins in fact support incoherent vibronic transport. This result points to an important design principle: Incoherent vibronic transport is more efficient than a coherent mechanism when energetic disorder exceeds the coupling between the donor and vibrationally excited acceptor states. Finally, our results suggest that the role of coherent vibronic transport in pigment protein complexes should be reevaluated

Molecular origins of induction and loss of photoinhibition-related energy dissipation qI

Photosynthesis fuels life on Earth using sunlight as energy source. However, light has a simultaneous detrimental effect on the enzyme triggering photosynthesis and producing oxygen, photosystem II (PSII). Photoinhibition, the light-dependent decrease of PSII activity, results in a major limitation to aquatic and land photosynthesis and occurs upon all environmental stress conditions. In this work, we investigated the molecular origins of photoinhibition focusing on the paradoxical energy dissipation process of unknown nature coinciding with PSII damage. Integrating spectroscopic, biochemical, and computational approaches, we demonstrate that the site of this quenching process is the PSII reaction center. We propose that the formation of quenching and the closure of PSII stem from the same event. We lastly reveal the heterogeneity of PSII upon photoinhibition using structure-function modeling of excitation energy transfer. This work unravels the functional details of the damage-induced energy dissipation at the heart of photosynthesis