Photosynthesis depends on light. However, excess light can be harmful for the photosynthetic apparatus because it produces reactive oxygen species (ROS) that cause photoinhibition. Oxygenic organisms evolved photoprotection mechanisms to counteract light-dependent ROS production, including preventive dissipation of excited states of chlorophyll (1Chl*) into heat in the process termed non-photochemical quenching (NPQ). This consists in the activation of 1Chl* quenching reactions when the thylakoid luminal pH drops below 5.2. In turn, acidification occurs when the rate of the CO2 reducing cycle is saturated and cannot regenerate ADP+Pi, thus inhibiting ATPase activity and the return of protons (H+) to the stromal compartment. The major and fastest component of NPQ is energy quenching, qE, which in algae depends on the Light-Harvesting Complex Stress-Related (LHCSR) proteins. In mosses, LHCSR proteins have remained the major catalysts of energy dissipation, but a minor contribution also occurs via a homologous protein, Photosystem II Subunit S (PSBS). In vascular plants, however, LHCSR has disappeared and PSBS is the only pH-sensitive trigger of qE. Why did PSBS replace LHCSR in the later stages of land colonization? Both PSBS and LHCSR belong to the Light Harvesting Complex superfamily (LHC) and share properties such as harboring protonatable residues that are exposed to the chloroplast lumen, which is essential for pH sensing. However, there are also conspicuous differences: LHCSR binds chlorophylls and xanthophylls while PSBS does not, implying that the former may well catalyse quenching reactions while the latter needs pigment-binding partners for its quenching function. Here, the evolution of quenching mechanisms for excess light is reviewed with a focus on the role of LHCSR versus PSBS, and the reasons for the redundancy of LHCSR in vascular plants as PSBS became established.

The rise and fall of Light-Harvesting Complex Stress-Related proteins as photoprotection agents during evolution

Pinnola, Alberta
Writing – Original Draft Preparation
2019-01-01

Abstract

Photosynthesis depends on light. However, excess light can be harmful for the photosynthetic apparatus because it produces reactive oxygen species (ROS) that cause photoinhibition. Oxygenic organisms evolved photoprotection mechanisms to counteract light-dependent ROS production, including preventive dissipation of excited states of chlorophyll (1Chl*) into heat in the process termed non-photochemical quenching (NPQ). This consists in the activation of 1Chl* quenching reactions when the thylakoid luminal pH drops below 5.2. In turn, acidification occurs when the rate of the CO2 reducing cycle is saturated and cannot regenerate ADP+Pi, thus inhibiting ATPase activity and the return of protons (H+) to the stromal compartment. The major and fastest component of NPQ is energy quenching, qE, which in algae depends on the Light-Harvesting Complex Stress-Related (LHCSR) proteins. In mosses, LHCSR proteins have remained the major catalysts of energy dissipation, but a minor contribution also occurs via a homologous protein, Photosystem II Subunit S (PSBS). In vascular plants, however, LHCSR has disappeared and PSBS is the only pH-sensitive trigger of qE. Why did PSBS replace LHCSR in the later stages of land colonization? Both PSBS and LHCSR belong to the Light Harvesting Complex superfamily (LHC) and share properties such as harboring protonatable residues that are exposed to the chloroplast lumen, which is essential for pH sensing. However, there are also conspicuous differences: LHCSR binds chlorophylls and xanthophylls while PSBS does not, implying that the former may well catalyse quenching reactions while the latter needs pigment-binding partners for its quenching function. Here, the evolution of quenching mechanisms for excess light is reviewed with a focus on the role of LHCSR versus PSBS, and the reasons for the redundancy of LHCSR in vascular plants as PSBS became established.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11571/1280206
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