Laboratoire de Photosynthèse et Métabolisme, Université de Paris-Sud, Centre d'Orsay, Bât. 430, F-91405, Orsay-Cedex, France.
Planta. 1985 Oct;166(2):187-93. doi: 10.1007/BF00397347.
Light activation of either NADP-malate dehydrogenase (EC 1.1.1.82) or fructose-1,6-bisphosphate phosphatase (EC 3.1.3.11) was assayed in a reconstituted chloroplastic, system comprising the isolated proteins of the ferredoxin-thioredoxin light-activation system and thylakoids from either mesophyll or bundle-sheath tissues of different C4 plants. While C4-plant thylakoids functionned almost equally well with C3-or C4-plant proteins, the photosyntem-II-deficient bundle-sheath thylakoids from the NADP-malic enzyme type, were unable to perform enzyme photoactivation unless supplemented with an electron donor to photosystem I. Bundle-sheath thylakoids isolated from plants showing no photosystem-II deficiency did not require such an addition. The results are discussed with respect to a possible requirement for a physiological reductant of ferredoxin for enzyme light activation in bundle-sheath, tissues.
在一个由分离的铁氧还蛋白-硫氧还蛋白光激活系统蛋白和来自不同 C4 植物的叶肉或束鞘组织的类囊体组成的重组叶绿体系统中,测定了 NADP-苹果酸脱氢酶(EC 1.1.1.82)或果糖-1,6-二磷酸磷酸酶(EC 3.1.3.11)的光激活。虽然 C4 植物类囊体与 C3 或 C4 植物蛋白的功能几乎相同,但 NADP-苹果酸酶型的缺乏光合系统 II 的束鞘类囊体,如果不补充给光系统 I 的电子供体,则无法进行酶的光激活。未表现出光合系统 II 缺陷的植物的束鞘类囊体不需要这种添加。结果与在束鞘组织中,铁氧还蛋白的酶光激活可能需要生理还原剂的假设有关。