Cannon G C, English R S, Shively J M
Department of Biological Sciences, Clemson University, South Carolina 29634.
J Bacteriol. 1991 Feb;173(4):1565-8. doi: 10.1128/jb.173.4.1565-1568.1991.
Cells permeabilized with chloroform yielded ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) activities nearly equal to those of cell extracts, thus indicating that both cytoplasmic and carboxysomal RuBisCO are functional in situ. The carboxysomal and cytoplasmic RuBisCO both form the CO2-Mg2(+)-enzyme ternary complex, as evidenced by stabilization with 2-C-carboxy-D-arabinitol-1,5-bisphosphate (CABP), a potent competitive inhibitor of RuBisCO. The data are consistent with the hypothesis that the carboxysome is functional in carbon dioxide fixation.
用氯仿透化处理的细胞产生的1,5-二磷酸核酮糖羧化酶/加氧酶(RuBisCO)活性几乎与细胞提取物的活性相当,这表明细胞质和羧基体中的RuBisCO在原位均具有功能。羧基体和细胞质中的RuBisCO都能形成CO₂-Mg²⁺-酶三元复合物,这一点通过用2-C-羧基-D-阿拉伯糖醇-1,5-二磷酸(CABP)(一种有效的RuBisCO竞争性抑制剂)进行稳定化处理得到了证明。这些数据与羧基体在二氧化碳固定中发挥作用的假设一致。