Biochemical and spectroscopic characterization of PSI-LHCI from the red alga Cyanidium caldarium

Biochemical and spectroscopic characterization of PSI-LHCI from the red alga Cyanidium caldarium
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红藻 Cyanidium caldarium 中 PSI-LHCI 的生化和光谱表征

DOI:
10.1007/s11120-023-00999-y
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发表时间:
2023
影响因子:
3.7
通讯作者:
Akimoto Seiji
Akimoto Seiji
中科院分区:
生物学3区
文献类型:
--
作者:
Nagao Ryo;Ueno Yoshifumi;Furutani Miyu;Kato Koji;Shen Jian-Ren;Akimoto Seiji

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捕光复合物(Light-harvesting complex,LHC)在光合生物中具有多样性,在捕获光能并将光能转移到两种类型的光系统核心以促进电荷分离反应中起着重要作用。红藻是光合作用的真核生物之一,其叶绿素(Chl)a结合的LHC与光系统I(PSI)特异性相关。在这项研究中,我们纯化了三种类型的制剂,PSI-LHCI超复合物,PSI核心,并从红藻Cyanidium caldarium分离LHCI,并检查其性能。PSI-LHCI的多肽条带显示了PSI和LHCI的特征成分,未被其他蛋白质污染。LHCI的类胡萝卜素组成显示玉米黄质、β-隐黄质和β-胡萝卜素。在类胡萝卜素中,玉米黄质在LHCI中富集。相反,玉米黄质和β-隐黄质都不能从PSI中检测到,这表明玉米黄质和β-隐黄质与LHCI结合,而不是PSI。与PSI和PSI-LHCI相比,LHCI的吸收光谱中Chlain的Qy峰向短波长移动。这一趋势与荧光发射光谱的结果一致,其中PSI-LHCI、PSI和LHCI的发射最大值分别出现在727、719和677 nm处。LHCI的时间分辨荧光光谱没有代表从皮秒到纳秒的719和727-nm荧光带。这些结果表明,通过将LHCI结合到PSI,改变LHCI周围/内和PSI内的Chls的能级。基于这些发现,我们讨论了红藻PSI-LHCI超复合物的表达,功能和结构。
Light-harvesting complexes (LHCs) have been diversified in oxygenic photosynthetic organisms, and play an essential role in capturing light energy which is transferred to two types of photosystem cores to promote charge-separation reactions. Red algae are one of the groups of photosynthetic eukaryotes, and their chlorophyll (Chl)a-binding LHCs are specifically associated with photosystem I (PSI). In this study, we purified three types of preparations, PSI-LHCI supercomplexes, PSI cores, and isolated LHCIs, from the red algaCyanidium caldarium, and examined their properties. The polypeptide bands of PSI-LHCI showed characteristic PSI and LHCI components without contamination by other proteins. The carotenoid composition of LHCI displayed zeaxanthins,β-cryptoxanthins, andβ-carotenes. Among the carotenoids, zeaxanthins were enriched in LHCI. On the contrary, both zeaxanthins andβ-cryptoxanthins could not be detected from PSI, suggesting that zeaxanthins andβ-cryptoxanthins are bound to LHCI but not PSI. A Qy peak of Chlain the absorption spectrum of LHCI was shifted to a shorter wavelength than those in PSI and PSI-LHCI. This tendency is in line with the result of fluorescence-emission spectra, in which the emission maxima of PSI-LHCI, PSI, and LHCI appeared at 727, 719, and 677 nm, respectively. Time-resolved fluorescence spectra of LHCI represented no 719 and 727-nm fluorescence bands from picoseconds to nanoseconds. These results indicate that energy levels of Chls around/within LHCIs and within PSI are changed by binding LHCIs to PSI. Based on these findings, we discuss the expression, function, and structure of red algal PSI-LHCI supercomplexes.
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