Zakharova N I, Permiakov E A, Fabian M, Kononenko A A, Chamorovskiĭ S K
Mol Biol (Mosk). 1984 May-Jun;18(3):719-24.
Luminescence emitted by tryptophan residues of reaction center (RC) preparations was studied. The RG preparations were isolated from the photosynthetic bacterium Rhodopseudomonas sphaeroides by treatment with lauryl dimethyl amine oxide (LDAO). After excitation at lambda 280 nm the quantum yield of luminescence is 0,02. It is shown that 60% of tryptophanyls are located inside the protein globule in the surrounding of relaxating polar groups and the rest approximately 40% on the outer surface of the globule--predominantly in the positively charged region of the LDAO-RC protein--in the surrounding of protein-bound water molecules. There is a correlation between the pH dependencies of the position of the peak of luminescence from tryptophanyls and effectivity of electron transfer from the primary (quinone) to secondary acceptor. The two parameters are invariant at pH from 7 to 9 and vary at pH less than 7 and pH greater than 9. The phenomena responsible for the observed correlation are discussed on the basis of pH-dependent changes in the RC protein which govern electron transport activity at the reaction center.
研究了反应中心（RC）制剂中色氨酸残基发出的荧光。通过用月桂基二甲基氧化胺（LDAO）处理，从光合细菌球形红假单胞菌中分离出RG制剂。在280nm波长激发后，发光量子产率为0.02。结果表明，60%的色氨酸位于蛋白质球内部，处于松弛极性基团的周围，其余约40%位于球的外表面——主要在LDAO-RC蛋白质的带正电区域——处于与蛋白质结合的水分子周围。色氨酸发光峰位置的pH依赖性与电子从初级（醌）受体向次级受体转移的效率之间存在相关性。这两个参数在pH值为7至9时不变，在pH值小于7和大于9时会发生变化。基于RC蛋白质中pH依赖性变化对反应中心电子传输活性的影响，讨论了导致观察到的相关性的现象。
