Pigment Interactions in Light-Harvesting Complex II in Different Molecular Environments.

Akhtar, Parveen and Dorogi, Márta and Pawlak, Krzyszof and Kovács, László and Bóta, Attila and Garab, Győző and Lambrev, Petar (2015) Pigment Interactions in Light-Harvesting Complex II in Different Molecular Environments. JOURNAL OF BIOLOGICAL CHEMISTRY, 290 (8). pp. 4877-4886. ISSN 0021-9258

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Abstract

Extraction of plant light-harvesting complex II (LHCII) from the native thylakoid membrane or from aggregates by the use of surfactants brings about significant changes in the excitonic circular dichroism (CD) spectrum and fluorescence quantum yield. To elucidate the cause of these changes, e.g. trimer-trimer contacts or surfactant-induced structural perturbations, we compared the CD spectra and fluorescence kinetics of LHCII aggregates, artificial and native LHCII-lipid membranes, and LHCII solubilized in different detergents or trapped in polymer gel. By this means we were able to identify CD spectral changes specific to LHCII-LHCII interactions - at (-)437 nm and (+)484 nm, and changes specific to the interaction with the detergent n-dodecyl-beta-maltoside (beta-DM) or membrane lipids - at (+)447 nm and ( )494 nm. The latter change is attributed to the conformational change of the LHCII-bound carotenoid neoxanthin, by analyzing the CD spectra of neoxanthin-deficient plant thylakoid membranes. The neoxanthin-specific band at ( )494 nm was not pronounced in LHCII in detergent-free gels or solubilized in the alpha isomer of DM but was present when LHCII was reconstituted in membranes composed of phosphatidylcholine or plant thylakoid lipids, indicating that the conformation of neoxanthin is sensitive to the molecular environment. Neither the aggrega-tion-specific CD bands, nor the surfactant-specific bands were positively associated with the onset of fluorescence quenching, which could be triggered without invoking such spec-tral changes. Significant quenching was not active in reconstituted LHCII proteoliposomes, while a high degree of energetic connectivity, depending on the lipid:protein ratio, in these membranes allows for efficient light harvesting.

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