Different carotenoid conformations have distinct functions in light-harvesting regulation in plants. Issue 1 (December 2017)

• Record Type: Journal Article
• Authors: Liguori, Nicoletta; Xu, Pengqi; Stokkum, Ivo H.M.; Oort, Bart; Lu, Yinghong; Karcher, Daniel; Bock, Ralph; Croce, Roberta
• Is Part Of: Nature communications. Volume 8:Issue 1(2017)
• Page Start: 1
• Page End: 9
• Publication Date: 2017-12
• Subjects: Biology -- Periodicals; Physical sciences -- Periodicals; 505
• DOI: 10.1038/s41467-017-02239-z
• Languages: English
• ISSNs: 2041-1723

Abstract

Abstract To avoid photodamage plants regulate the amount of excitation energy in the membrane at the level of the light-harvesting complexes (LHCs). It has been proposed that the energy absorbed in excess is dissipated via protein conformational changes of individual LHCs. However, the exact quenching mechanism remains unclear. Here we study the mechanism of quenching in LHCs that bind a single carotenoid species and are constitutively in a dissipative conformation. Via femtosecond spectroscopy we resolve a number of carotenoid dark states, demonstrating that the carotenoid is bound to the complex in different conformations. Some of those states act as excitation energy donors for the chlorophylls, whereas others act as quenchers. Via in silico analysis we show that structural changes of carotenoids are expected in the LHC protein domains exposed to the chloroplast lumen, where acidification triggers photoprotection in vivo. We propose that structural changes of LHCs control the conformation of the carotenoids, thus permitting access to different dark states responsible for either light harvesting or photoprotection. Carotenoids can dissipate excess energy captured by photosynthetic light-harvesting complexes to prevent photodamage. Here, via spectroscopic and in silico approaches, Liguori et al. resolve different carotenoid dark states and propose conformational changes that permit them to act as either energy donors or quenchers.