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Photosynth Res. 1996 Jan;47(1):1-11. doi: 10.1007/BF00017748.

The mechanism of Rubisco activase: Insights from studies of the properties and structure of the enzyme.

Author information

1
Western Cotton Research Laboratory, United States Department of Agriculture-Agricultural Research Service, 4135 E. Broadway Road, 85040-8830, Phoenix, AZ.

Abstract

Rubisco, the primary carboxylating enzyme in photosynthesis, must be activated to catalyze CO2 fixation. The concept of an 'activase', a specific protein for activating Rubisco, was first introduced in 1985 based largely on biochemical and genetic studies of a high CO2-requiring mutant of Arabidopsis (Salvucci et al. (1985) Photosynth Res 7: 193-201). Over the past ten years, details about the occurrence, structure, and properties of Rubisco activase have been elucidated. However, the mechanism of action of Rubisco activase remains elusive. This review discusses the need for and function of Rubisco activase and summarizes information about the properties and structure of Rubisco activase. The information is evaluated in the context of the mechanism of Rubisco activase.

PMID:
24301702
DOI:
10.1007/BF00017748

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