EC Number   |
General Information |
Reference |
|---|
   1.3.7.7 | physiological function |
during chlorophyll biosynthesis in photosynthetic bacteria, cyanobacteria, green algae and gymnosperms, dark-operative protochlorophyllide oxidoreductase, a nitrogenase-like metalloenzyme, catalyzes the chemically challenging two-electron reduction of the fully conjugated ring system of protochlorophyllide a. The reduction of the C-17=C-18 double bond results in the characteristic ring architecture of all chlorophylls, thereby altering the absorption properties of the molecule and providing the basis for light-capturing and energytransduction processes of photosynthesis |
726394 |
| 1.3.7.7 | physiological function |
light-independent protochlorophyllide reductase is required for protochlorophyllide reduction in the dark |
672764 |
| 1.3.7.7 | physiological function |
the expression of NADPH:protochlorophyllide oxidoreductase A (PorA), PorB, and PorC, which catalyze a key step in chlorophyll biosynthesis, is increased in the BRM mutants, defective in a SWI2/SNF2 chromatin-remodeling ATPase |
743315 |
