pH-Responsive Binding Properties of Light-Harvesting Complexes in a Photosystem II Supercomplex Investigated by Thermodynamic Dissociation Kinetics Analysis

被引：9
|
作者：
Kim, Eunchul [1 ]
Watanabe, Akimasa [1 ,2 ]
Sato, Ryoichi [1 ]
Okajima, Keisuke [1 ,2 ]
Minagawa, Jun [1 ,2 ]
机构：
[1] Natl Inst Basic Biol, Div Environm Photobiol, Okazaki, Aichi 4448585, Japan
[2] Grad Univ Adv Studies, Dept Basic Biol, Sch Life Sci, Okazaki, Aichi 4448585, Japan
来源：
JOURNAL OF PHYSICAL CHEMISTRY LETTERS | 2019年 / 10卷 / 13期
基金：
日本学术振兴会;
关键词：
PHOTOPROTECTIVE ENERGY-DISSIPATION; GRANA MEMBRANES; CORE ANTENNA; PSBS PROTEIN; ORGANIZATION; MECHANISM; AMPHIPOLS; DYNAMICS; CP47;
D O I：
10.1021/acs.jpclett.9b01208
中图分类号：
O64 [物理化学（理论化学）、化学物理学];
学科分类号：
070304 ; 081704 ;
摘要：
Reorganization of photosynthetic proteins on the thylakoid membrane is an important regulatory process for photoacclimation in photosynthetic organisms. However, the underlying mechanism has been poorly understood due to the lack of methods to analyze the interactions between membrane proteins. To investigate the mechanism, we demonstrated the binding properties of light-harvesting complex proteins (LHCs) in a photosystem II (PSII) supercomplex regulated by pH conditions, which primarily responded to environmental light conditions, using a thermodynamic dissociation kinetics analysis. The results showed that the strongly bound LHCs (similar to 60%) were responsive to pH conditions, whereas the moderately and loosely bound LHCs (similar to 40%) were nonresponsive. This result implies that the pH condition alters the binding properties of LHCs in the PSII supercomplex, inducing the reorganization of protein complexes.
引用
收藏
页码：3615 / 3620
页数：11
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