A power-law relationship
between kcat,C/KC and kcat,O/KO can be explained by an active site
that fluctuates between “reactive” and “unreactive”
states. (A) In this model, CO2 and O2 react
with bound RuBP only when the enzyme is in the reactive state, which
has an occupancy φ. (B) φ can vary between related enzymes.
In the reactive state, CO2 and O2 react with
the bound RuBP with intrinsic reactivities ΔG*1,C and ΔG*1,O that
do not vary between related Rubiscos. If the difference in intrinsic
reactivities (ΔG*1,O – ΔG*1,C) is constant, we derive a power-law
relationship between kcat,C/KC and kcat,O/KO with an exponent of 1.0. This relationship requires
a constant SC/O (Supporting Information).