Regulating energy transfer in the ATP sulfurylase-GTPase system

A study was conducted on the transience that is observed during the regulation of energy transfer in the ATP sulfurylase-GTPase system. The findings indicate that Pi binding directs the system through the coupled mechanism and that the mass ratio of the activated sulfate (APS) reaction can be tuned by adjusting flux through the coupled and uncoupled pathways. Moreover, this coupling mechanism provides an approach for controlling the quantity of chemical potential transferred to the APS reaction.