分离的 FMO 蛋白和来自绿硫细菌 Chlorobium tepidum 的无膜反应中心复合物的低温光谱。
Low-temperature spectroscopy of isolated FMO-protein and a membrane-free reaction center complex from the green sulfur bacteriumChlorobium tepidum.
机构信息
Institute of Biochemistry, Odense University, Campusvej 55, DK-5230, Odense M, Denmark.
出版信息
Photosynth Res. 1994 Jul;41(1):97-103. doi: 10.1007/BF02184149.
We have isolated the water-soluble BChla-protein (FMO-protein) from the greer sulfur bacteriumChlorobium tepidum by a new procedure involving a salt-wash of isolated membranes at alkaline pH. The absorption spectrum of the isolated FMO-protein at 77 K was compared with that of a reaction-center complex containing the FMO-protein (FMO-RC complex) isolated fromC. tepidum following the procedure of Feiler U, Nitsche W and Michel H (1992) Biochemistry 31: 2608-2614. Oxidation or illumination of the FMO-RC complex caused bleaching of a component with a maximum at 836 nm which was not present in the purified FMO-protein.
我们通过一种新的方法从绿硫细菌（Chlorobium tepidum）中分离出水溶性 BChla 蛋白（FMO 蛋白），该方法涉及在碱性 pH 值下对分离的膜进行盐洗。在 77 K 下，分离的 FMO 蛋白的吸收光谱与 Feiler U、Nitsche W 和 Michel H（1992）生物化学 31:2608-2614 中所述的从 C. tepidum 中分离出的含有 FMO 蛋白的反应中心复合物（FMO-RC 复合物）的吸收光谱进行了比较。FMO-RC 复合物的氧化或光照导致在 836nm 处出现最大峰的一个组分的漂白，而在纯化的 FMO 蛋白中不存在该组分。
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