Conformation of Light-Harvesting Complex II Trimer Depends upon Its Binding Site

Autor:	Eunchul Kim, Hisako Kubota-Kawai, Fumihiro Kawai, Makio Yokono, Jun Minagawa
Rok vydání:	2022
Předmět:	Chlorophyll Binding Sites Light-Harvesting Protein Complexes Materials Chemistry Photosystem II Protein Complex Plants Physical and Theoretical Chemistry Chlamydomonas reinhardtii Surfaces Coatings and Films
Zdroj:	The Journal of Physical Chemistry B. 126:5855-5865
ISSN:	1520-5207 1520-6106
DOI:	10.1021/acs.jpcb.2c04061
Popis:	The light-harvesting complex II (LHCII) trimer in plants functions as a major antenna complex and a quencher to protect it from photooxidative damage. Theoretical studies on the structure of an LHCII trimer have demonstrated that excitation energy transfer between chlorophylls (Chls) in LHCII can be modulated by its exquisite conformational fluctuation. However, conformational changes depending on its binding location have not yet been investigated, even though reorganization of protein complexes occurs by physiological regulations. In this study, we investigated conformational differences in LHCII by comparing published structures of an identical LHCII trimer in the three different photosystem supercomplexes from the green alga
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d7c62fa7430b85bf7c668fd596d02277 https://doi.org/10.1021/acs.jpcb.2c04061 Zobrazit plný text záznamu