  In this work we study, at the single molecular level, the thermodynamic and
dynamic characteristics of an enzymatic reaction comprising a rate limiting
step. We investigate how the stability of the enzyme-state stationary
probability distribution, the reaction velocity, and its efficiency of energy
conversion depend on the system parameters. We employ in this study a recently
introduced formalism for performing a multiscale thermodynamic analysis in
continuous-time discrete-state stochastic systems.
