Departamento de Bioquímica y Biología Molecular y Celular, Facultad de Ciencias, Universidad de Zaragoza, Spain.
Photosynth Res. 1993 Oct;38(1):35-9. doi: 10.1007/BF00015059.
Flavodoxin from the cyanobacterium Anabaena PCC 7119 has been shown to mediate, under illumination, the transfer of electrons from the thylakoidal membranes that were isolated from the same organism, to both the enzyme ferredoxin-NADP(+) reductase and cytochrome c. Chemical cross-linking of ferredoxin or flavodoxin to the photosynthetic membranes provides a preparation that is active in cytochrome c photoreduction without the addition of external protein carrier. NADP(+) photoreduction, albeit diminished, was observed only after addition of exogenous electron carrier protein. Immunoblotting analysis of the chemical adduct reveals that flavodoxin binds to a 10 kDa polypeptide subunit in the cyanobacterial Photosystem I which appears to act as its physiological partner in the electron transfer process.
从蓝藻鱼腥藻 PCC 7119 中分离出的黄素蛋白被证明能够在光照下介导电子从分离自同一生物体的类囊体膜转移到酶ferredoxin-NADP(+)还原酶和细胞色素 c。将 ferredoxin 或 flavodoxin 化学交联到光合膜上，提供了一种在不添加外部蛋白载体的情况下可使细胞色素 c 光还原的制剂。只有在外源电子载体蛋白添加后，才观察到 NADP(+)光还原，尽管还原程度降低。化学加合物的免疫印迹分析表明，黄素蛋白与蓝细菌光系统 I 中的 10 kDa 多肽亚基结合，该亚基似乎在电子传递过程中作为其生理伴侣。
