期刊
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
卷 1863, 期 7, 页码 -出版社
ELSEVIER
DOI: 10.1016/j.bbabio.2022.148584
关键词
Cyanobacteria; Flash photolysis; Photosynthetic pigments; Structure function relationships; X-ray diffraction
资金
- CEA
- CNRS
- Universite Grenoble Alpes
- Universite Paris-Saclay
- Agence Nationale de la Recherche [ANR-17-CE11-0018-01, ANR-2018-CE11-0005-02]
- Polish National Science Centre (NCN) [2018/31/N/ST4/03983]
- FRISBI [ANR-10-INBS-05-02]
- GRAL, a project of the University Grenoble Alpes graduate school ('Ecoles Universitaires de Recherche) CBH-EUR-GS [ANR-17-EURE-0003]
- Agence Nationale de la Recherche (ANR) [ANR-17-CE11-0018] Funding Source: Agence Nationale de la Recherche (ANR)
This study reports on the characteristics of Plankto-OCP, a variant of the orange carotenoid protein (OCP) involved in cyanobacterial photoprotection. Plankto-OCP shows higher photoactivation and recovery rates, stronger energy-quenching activity, and is affected by the presence of a his-tag and the functionalizing carotenoid. The structures of Plankto-OCP reveal its molecular breathing motions and potential structural changes that explain its unique properties.
The orange carotenoid protein (OCP) is a photoactive protein involved in cyanobacterial photoprotection. Here, we report on the functional, spectral and structural characteristics of the peculiar Planktothrix PCC7805 OCP (Plankto-OCP). We show that this OCP variant is characterized by higher photoactivation and recovery rates, and a stronger energy-quenching activity, compared to other OCP studied thus far. We characterize the effect of the functionalizing carotenoid and of his-tagging on these reactions, and identify the time scales on which these modifications affect photoactivation. The presence of a his-tag at the C-terminus has a large influence on photoactivation, thermal recovery and PBS-fluorescence quenching, and likewise for the nature of the carotenoid that additionally affects the yield and characteristics of excited states and the ns-s dynamics of photoactivated OCP. By solving the structures of Plankto-OCP in the ECN- and CAN-functionalized states, each in two closelyrelated crystal forms, we further unveil the molecular breathing motions that animate Plankto-OCP at the monomer and dimer levels. We finally discuss the structural changes that could explain the peculiar properties of Plankto-OCP.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据