Copyright © 2002 Elsevier Science B.V. All rights reserved.
Single-molecule enzymology: stochastic Michaelis–Menten kinetics
Received 23 January 2002;
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Abstract
We provide a stochastic analysis of single-molecule enzymatic reactions that follow Michaelis–Menten kinetics. We show that this system can exhibit oscillatory behavior in the non-equilibrium steady-state at appropriate substrate concentrations. The stochastic model includes both enzyme dynamics and substrate turnover kinetics. The relationship between the probability of substrate survival and the time-correlation of enzyme conformation trajectories is discussed. Deterministic kinetics at large substrate concentrations are obtained as a limit of the stochastic model. We suggest that in addition to fluctuating enzyme conformation, the stochastic nature of substrate concentration fluctuations is another possible source of the complex behavior of single-molecule enzyme kinetics.
Author Keywords: Stochastic analysis; Oscillatory behaviour; Non-equilibrium; Enzyme dynamics; Deterministic kinetics
Article Outline
- 1. Introduction
- 2. Non-equilibrium steady-state enzyme turnover
- 3. Stochastic substrate kinetics
- 4. Discussion
- Appendix A. Higher-order correlation functions for two-state kinetics
- Appendix B. Real eigenvalues in equilibrium
- Appendix C. Distribution and moments of substrate fluctuation
- Appendix D. Duality between mean arrival time and steady-state cyclic flux
- References







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