Khristin M S, Akulova E A, Surovtsev V I
Biokhimiia. 1977 Jan;42(1):124-8.
Cytochrome c immobilized on cyanogen bromide-activated Sepharose 4B may be used to study photochemical reactions in chloroplasts. Chloroplast reduction of both immobilized and soluble forms of the cytochrome occurs along the exogenous and endogenous pathways which results in a weaker reduction of the immobilized protein as compared to that of the soluble one. The time of the reduced immobilized cytochrome c oxidation in the dark is two orders of magnitude greater than that of the soluble one. This fact may be interpreted in terms of spatial dissociation of reductase and oxidase centers of chloroplasts with reference to the cytochrome. The optimal ionic strength for cytochrome reduction, i.e. ionic strength causing an in vitro destruction of the ferredoxin-NADP-reductase complex was found to equal to 0.2 M.
固定在溴化氰活化的琼脂糖凝胶4B上的细胞色素c可用于研究叶绿体中的光化学反应。叶绿体对固定化和可溶性形式的细胞色素的还原沿着外源和内源途径发生，与可溶性细胞色素相比，固定化蛋白质的还原较弱。黑暗中还原的固定化细胞色素c氧化的时间比可溶性细胞色素c的氧化时间大两个数量级。这一事实可以从叶绿体还原酶和氧化酶中心相对于细胞色素的空间解离来解释。发现细胞色素还原的最佳离子强度，即导致铁氧还蛋白-NADP还原酶复合物在体外破坏的离子强度等于0.2M。
