Abstract
Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is an enzyme that catalyzes the carboxylation of the substrate Ribulose-1,5-bisphosphate. The notorious inefficiency of RuBisCO to catalyze carboxylation is due to inhibition by various metabolites. RuBisCO activase, an ancillary enzyme is needed to foster the activity of RuBisCO. Activase has been recognized as a member of the AAA+ family of the ATPases. It facilitates the removal of firmly bound sugar phosphates thereby restoring RuBisCO activity. The stoichiometry and oligomerization kinetics of fluorescently tagged RuBisCO activase was investigated in a wide range of concentrations using Fluorescence Correlation Spectroscopy (FCS) in conjunction with Photon counting Histogram (PCH) analysis. Experiments revealed that Activase exists as a monomer at sub-micro molar concentrations, and assembles into oligomers (possible hexamers) at higher concentrations. The analysis of the concentration-dependent diffusion coefficient revealed that the binding between the subunits occurs in steps involving intermediates. The pathway of assembly taken by Activase was found to be independent of the presence of ATP-γS or ADP in the system.
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