Wildner G F
Z Naturforsch C Biosci. 1975 Nov-Dec;30(6):756-60. doi: 10.1515/znc-1975-11-1211.
Glucose-6-phosphate dehydrogenase from intact pea chloroplasts is partially membrane bound and inactivated upon illumination. The inhibitory effect of light can be abolished by addition of methylviologen. Kinetic experiments with glucose-6-phosphate dehydrogenase reveal that, in the dark, the enzyme activity is strongly inhibited by the accumulation of NADPH. The inhibition of NADPH can be reversed by the addition of excess NADP+. The non-Michaelis-Menten-type kinetics suggest that the enzyme is stringently regulated by the ratio of NADPH to NADP+ plus NADPH, i.e., the "reduction charge". These observations seem to indicate that in the light the inhibition of glucose-6-phosphate dehydrogenase is due to a high reduction charge, whereas in the dark the enzyme is controlled by the metabolic demand for reducing equivalents.
完整豌豆叶绿体中的葡萄糖-6-磷酸脱氢酶部分与膜结合，并在光照下失活。添加甲基紫精可消除光的抑制作用。对葡萄糖-6-磷酸脱氢酶进行的动力学实验表明，在黑暗中，该酶的活性受到NADPH积累的强烈抑制。添加过量的NADP+可逆转NADPH的抑制作用。非米氏动力学类型表明，该酶受到NADPH与NADP+加NADPH的比例（即“还原电荷”）的严格调节。这些观察结果似乎表明，在光照下，葡萄糖-6-磷酸脱氢酶的抑制是由于高还原电荷，而在黑暗中，该酶则受代谢对还原当量需求的控制。
