Bieth J, Vratsanos S M, Wassermann N, Erlanger B F
Proc Natl Acad Sci U S A. 1969 Nov;64(3):1103-6. doi: 10.1073/pnas.64.3.1103.
The enzymic activity of acetylcholinesterase can be photoregulated through the mediation of photochromic inhibitors of the enzyme. N-p-phenylazophenyl-N-phenylcarbamyl fluoride, an irreversible inhibitor of acetylcholinesterase, exists as two geometric isomers which are interconvertible through the action of light. The cis isomer, which predominates after exposure to light of 320 nm, is more active than the trans isomer, which results from exposure to light of 420 nm. It was possible, therefore, to use light energy to regulate the inactivation of the enzyme. Similarly, levels of acetylcholinesterase activity could be photo-regulated in a completely reversible manner by means of the photochromic reversible inhibitor p-phenylazophenyltrimethylammonium chloride. These experiments can serve as models for similar phenomena observed in nature, particularly in photoperiodic rhythms of higher animals.
乙酰胆碱酯酶的酶活性可通过该酶的光致变色抑制剂介导进行光调节。N-对苯基偶氮苯基-N-苯基氨基甲酰氟是乙酰胆碱酯酶的一种不可逆抑制剂，它以两种几何异构体的形式存在，这两种异构体可通过光的作用相互转化。顺式异构体在暴露于320nm光后占主导，比反式异构体更具活性，反式异构体是在暴露于420nm光后产生的。因此，利用光能调节该酶的失活成为可能。同样，借助光致变色可逆抑制剂对苯基偶氮苯基三甲基氯化铵，乙酰胆碱酯酶的活性水平可以完全可逆的方式进行光调节。这些实验可作为自然界中观察到的类似现象的模型，特别是在高等动物的光周期节律中。
