Biology Department, Brookhaven National Laboratory, Upton, New York 11973.
Proc Natl Acad Sci U S A. 1980 Apr;77(4):1961-5. doi: 10.1073/pnas.77.4.1961.
Phycobilisomes are supramolecular assemblies of phycobiliproteins responsible for photosynthetic light collection in red algae and cyanobacteria. They can be selectively dissociated by reduction of temperature and buffer concentration. Phycobilisomes isolated from Fremyella diplosiphon transfer energy collected by C-phycoerythrin and C-phycocyanin to allophycocyanin. The energy transfer to allophycocyanin is nearly abolished at 2 degrees C, as indicated by a blue shift in fluorescence emission, and is accompanied by a decrease in the circular dichroism in the region of allophycocyanin absorbance. Further dissociation of the phycobilisomes can be attained by reduction of buffer concentration and holding at 2 degrees C. Energy transfer to C-phycocyanin is nearly abolished, and decreases occur in the circular dichroism in the region of C-phycocyanin and C-phycoerythrin absorbance. Complete dissociation of the phycobilisomes at low buffer concentration and 2 degrees C requires extended time. Energy transfer to C-phycocyanin is further reduced and the circular dichroism maximum of C-phycoerythrin at 575 nm is lost. Circular dichroism provides information on the hexamer-monomer transitions of the phycobiliproteins, whereas fluorescence is indicative of hexamer-hexamer interactions. We consider that hydrophobic interactions are fundamental to the maintenance of the structure and function of phycobilisomes.
藻胆体是负责红藻和蓝藻光合作用光收集的藻胆蛋白的超分子组装体。它们可以通过降低温度和缓冲浓度选择性地解离。从 Fremyella diplosiphon 中分离出的藻胆体将 C-藻红蛋白和 C-藻蓝蛋白收集的能量转移到别藻蓝蛋白。如荧光发射的蓝移所示,在 2°C 时,能量向别藻蓝蛋白的转移几乎被完全抑制,并伴有别藻蓝蛋白吸收区圆二色性的降低。通过降低缓冲浓度并保持在 2°C 可以进一步解离藻胆体。向 C-藻蓝蛋白的能量转移几乎被完全抑制,并且在 C-藻蓝蛋白和 C-藻红蛋白吸收区的圆二色性降低。在低缓冲浓度和 2°C 下完全解离藻胆体需要延长时间。向 C-藻蓝蛋白的能量转移进一步减少,并且 575nm 处 C-藻红蛋白的圆二色性最大值消失。圆二色性提供了关于藻胆蛋白六聚体-单体转变的信息,而荧光则表明六聚体-六聚体相互作用。我们认为疏水性相互作用是维持藻胆体结构和功能的基础。