The observed 90∘+30∘ substeps sum to 120∘, consistent with three catalytic cycles per revolution of F1-ATPase. Surface attachment fixes the β-subunit frame while the gold-labelled γ shaft reports relative rotation. A finite dwell before the smaller step indicates hidden chemical transitions rather than a completely smooth motor.
Suppose two irreversible independent first-order transitions, with rates ka and kb, must occur sequentially before the 30∘ step. Their waiting times Xa and Xb have exponential distributions, and τ=Xa+Xb. Convolution gives
This probability density integrates to one and has ⟨τ⟩=ka−1+kb−1. For equal rates its continuous limit is P(τ)=k2τe−kτ, not asingular distribution. In particular P(0)=0 distinguishes two resolved sequential waits from a single exponential wait. Hydrolysis and product release are plausible underlying chemical events, but the waiting-time fit alone neither assigns their order nor uniquely identifies which biochemical eventcauses each substep. Concentration dependence or independent labelling would be needed for that assignment.