Tang X S, Fushimi K, Satoh K
Department of Biology, Faculty of Science, Okayama University, Japan.
FEBS Lett. 1990 Oct 29;273(1-2):257-60. doi: 10.1016/0014-5793(90)81098-9.
A pigment-protein complex consisting of D1 and D2 proteins, but depleted in the two lower molecular mass components of photosystem II, i.e. cytochrome b-559 and psbI gene product, has been isolated by octyl-beta-D-glucopyranoside treatment of the purified photosystem II reaction center complex from spinach [(1987) Proc. Natl. Acad. Sci. USA 84, 109-112], followed by separation by high performance liquid chromatography using a gel-permeation column (TSK G3000 SW). The isolated complex is photochemically active in the photoreduction of intrinsic pheophytin a under steady-state illumination, in the presence of dithionite and methyl viologen, and exhibits pigment stoichiometries similar to those in the untreated reaction center, indicating that the D1-D2 complex provides the site of primary photochemistry in photosystem II, as well as the principal binding sites of pigments in the reaction center.
一种由D1和D2蛋白组成的色素-蛋白复合物，它缺乏光系统II的两个较低分子量组分，即细胞色素b-559和psbI基因产物。通过用辛基-β-D-吡喃葡萄糖苷处理菠菜纯化的光系统II反应中心复合物[（1987年）美国国家科学院院刊84, 109 - 112]，然后使用凝胶渗透柱（TSK G3000 SW）通过高效液相色谱进行分离，从而分离得到该复合物。在连二亚硫酸盐和甲基紫精存在的稳态光照下，分离得到的复合物在其内在脱镁叶绿素a的光还原中具有光化学活性，并且表现出与未处理反应中心相似的色素化学计量比，这表明D1-D2复合物提供了光系统II中初级光化学的位点以及反应中心中色素的主要结合位点。
