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Understanding the molecular mechanisms that make enzymes work remains one of the grand challenges in contemporary biophysics. If this understanding can be translated into the successful re-engineering of enzymes with greater efficiency, the practical benefits could be enormous. One such enzyme that has been targeted for re-engineering, ribulose 1,5-bisphosphate carboxylase/ oxygenase (Rubisco, EC 4.1.1.39), is of intensive interest in agriculture and related fields as it fixes CO2 in higher plants and the vast majority of other photosynthetic organisms. In a recent article, Cummins et al. (2018a), we presented a statistical analysis of a wide range of published kinetic data on Rubisco. The results of that study suggested evidence of significant rates of decarboxylation (reaction with CO2) and deoxygenation (from the side reaction of Rubisco with O2) among wild-type Rubiscos. These results have challenged the accepted view that dissociation of the gas molecules (decarboxylation and deoxygenation) from the enzyme complex is negligible in all wildtype Rubiscos. In a commentary on Cummins et al. (2018a), Tcherkez et al. (2018) have contested our conclusion of significant decarboxylation and deoxygenation rates in Rubisco and suggested it is based on a misinterpretation of “implicit relationships between Rubisco rate constants” and “overlooks experimental evidence for feeble rates of deoxygenation and decarboxylation.” In this response to their commentary on Cummins et al. (2018a), we address these criticisms.

Response: Commentary: Directions for Optimization of Photosynthetic Carbon Fixation: RuBisCO’s Efficiency May Not Be So Constrained After All