Molecular mechanism of Rubisco activase: Dynamic assembly and Rubisco remodeling

Kazi Waheeda, Heidi Kitchel, Quan Wang, Po Lin Chiu

Research output: Contribution to journalShort surveypeer-review

5 Scopus citations


Ribulose-1,5-bisphosphate (RuBP) carboxylase-oxygenase (Rubisco) enzyme is the limiting step of photosynthetic carbon fixation, and its activation is regulated by its co-evolved chaperone, Rubisco activase (Rca). Rca removes the intrinsic sugar phosphate inhibitors occupying the Rubisco active site, allowing RuBP to split into two 3-phosphoglycerate (3PGA) molecules. This review summarizes the evolution, structure, and function of Rca and describes the recent findings regarding the mechanistic model of Rubisco activation by Rca. New knowledge in these areas can significantly enhance crop engineering techniques used to improve crop productivity.

Original languageEnglish (US)
Article number1125922
JournalFrontiers in Molecular Biosciences
StatePublished - Feb 10 2023


  • AAA+ ATPase
  • Rubisco
  • Rubisco activase
  • carbon fixation
  • photosynthesis
  • redox

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology (miscellaneous)


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