The roles of a light-dependent protochlorophyllide oxidoreductase (LPOR), and ATP-dependent dark operative protochlorophyllide oxidoreductase (DPOR) in chlorophyll biosynthesis


  • Wenli SUN Chinese Academy of Agricultural Sciences, Biotechnology Research Institute, Beijing 100081 (CN)
  • Mohamad H. SHAHRAJABIAN Chinese Academy of Agricultural Sciences, Biotechnology Research Institute, Beijing 100081 (CN)
  • Qi CHENG State Key Laboratory of North China Crop Improvement and Regulation, Hebei Agricultural University, College of Life Sciences, Baoding, Hebei 071000, China; Global Alliance of HeBAU-CLS&HeQiS for BioAl-Manufacturing, College of Life Sciences, Hebei Agricultural University, Baoding, 071000 (CN)



chlorophyll, chlorophyllide, DPOR, LPOR, protochlorophyllide oxidoreductase


Chlorophyll is a green photosynthetic pigment, and photosynthesis drives the global carbon cycle. The reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide) in the penultimate stage of biosynthesis of chlorophyll (Chl) is catalyzed by light-independent protochlorophyllide reducatse (DPOR), and the light-dependent protochlorophyllide oxidoreductase (LPOR). The search was done to all manuscript sections according to terms chlorophyll, a light-dependent protochlorophyllide oxidoreductase, ATP-dependent dark operative protochlorophyllide oxidoreductase, chlorophyll, photosynthesis and chlorophyllide. Within the framework of photosynthesis and chlorophyll, this review article was aimed to provide an overview of the functional studies in chlorophyll biosynthesis, protein crystal structure, disclosure of action mechanisms, and possible future available direction of LPOR and DPOR in the biosynthesis of chlorophyll.


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How to Cite

SUN, W., SHAHRAJABIAN, M. H., & CHENG, Q. (2021). The roles of a light-dependent protochlorophyllide oxidoreductase (LPOR), and ATP-dependent dark operative protochlorophyllide oxidoreductase (DPOR) in chlorophyll biosynthesis. Notulae Botanicae Horti Agrobotanici Cluj-Napoca, 49(3), 12456.



Review Articles
DOI: 10.15835/nbha49312456