Absence of the third linker domain of ApcE subunit in phycobilisome from Synechocystis 6803 reduces rods-to-core excitation energy transfer.

IF 2.3 3区 化学 Q3 CHEMISTRY, PHYSICAL Chemphyschem Pub Date : 2024-11-05 DOI:10.1002/cphc.202400933
Dariusz Niedzwiedzki, Rupal Singh Tomar, Fatima Akram, Anna M Williams, Haijun Liu
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Abstract

Phycobilisome (PBS) is a pigment-protein complex utilized by red algae and cyanobacteria in photosynthesis for light harvesting. A cyanobacterium Synechocystis sp. PCC 6803 contains PBS with a tricylindrical core built of allophycocyanin (APC) disks where six phycocyanin (PC) rods are attached. The top core cylinder is seemingly involved in attaching four PC rods and binding orange carotenoid protein (OCP) to quench excess of excitation energy. In this study, we have deleted the third linker domain (LD3) of ApcE subunit of PBS which assembles four APC discs into the top core cylinder. The mutation resulted in PBS with bicylindrical core, structurally comparable to the naturally existing PBS from Synechococcus 7942. Lack of LD3 and the top APC cylinder reduces the excitation energy transfer between PC and APC in the mutant. Moreover, these PBSs are more prone to light induced-photodamage and do not bind to the photoactivated orange carotenoid protein (OCP), a known PBS excitation quencher. These findings highlight the complex and elegant interplay between PBS architecture and functional efficiency, suggesting that in PBSs with naturally tri-cylindrical cores, the top cylinder has essential roles in recruiting the rods and proper binding of OCP and recruitment of the four PC rods.

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Synechocystis 6803 的噬菌体中 ApcE 亚基第三连接域的缺失减少了棒-核激发能量的传递。
藻青素体(PBS)是红藻和蓝藻在光合作用中用于采光的色素-蛋白质复合体。蓝藻 Synechocystis sp. PCC 6803 含有一个由异叶绿素(APC)盘构成的三圆柱形核心 PBS,其中连接着六根藻蓝蛋白(PC)棒。顶端的核心圆柱体似乎参与连接四根 PC 棒,并结合橙色类胡萝卜素蛋白(OCP)以熄灭过量的激发能量。在这项研究中,我们删除了 PBS 的 ApcE 亚基的第三个连接子结构域(LD3),该结构域将四个 APC 圆盘组装到顶核圆柱体中。这一突变导致 PBS 具有双圆柱形核心,在结构上与来自 Synechococcus 7942 的天然 PBS 相似。由于缺少 LD3 和顶部 APC 圆柱,突变体中 PC 和 APC 之间的激发能量转移减少。此外,这些 PBS 更容易受到光诱导的光损伤,并且不能与光激活的橙色类胡萝卜素蛋白(OCP)结合,而 OCP 是一种已知的 PBS 激发淬灭剂。这些发现突显了 PBS 结构与功能效率之间复杂而优雅的相互作用,表明在具有天然三圆柱形核心的 PBS 中,顶圆柱在招募杆状体、正确结合 OCP 和招募四个 PC 杆状体方面具有重要作用。
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来源期刊
Chemphyschem
Chemphyschem 化学-物理:原子、分子和化学物理
CiteScore
4.60
自引率
3.40%
发文量
425
审稿时长
1.1 months
期刊介绍: ChemPhysChem is one of the leading chemistry/physics interdisciplinary journals (ISI Impact Factor 2018: 3.077) for physical chemistry and chemical physics. It is published on behalf of Chemistry Europe, an association of 16 European chemical societies. ChemPhysChem is an international source for important primary and critical secondary information across the whole field of physical chemistry and chemical physics. It integrates this wide and flourishing field ranging from Solid State and Soft-Matter Research, Electro- and Photochemistry, Femtochemistry and Nanotechnology, Complex Systems, Single-Molecule Research, Clusters and Colloids, Catalysis and Surface Science, Biophysics and Physical Biochemistry, Atmospheric and Environmental Chemistry, and many more topics. ChemPhysChem is peer-reviewed.
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