相关论文: The Michaelis-Menten-Stueckelberg Theorem

The rates of chemical reactions are not absolute but their magnitude depends upon the relative speeds of the moving observers. This has been proved by unifying theories of chemical kinetics, which are transition state theory, collision…

All biological processes are controlled by complex systems of enzymatic chemical reactions. Although the majority of enzymatic networks have very elaborate structures, there are many experimental observations indicating that some turnover…

The conditions for the validity of the standard quasi-steady-state approximation in the Michaelis--Menten mechanism in a closed reaction vessel have been well studied, but much less so the conditions for the validity of this approximation…

We extend Araki's well-known results on the equivalence of the KMS condition and the variational principle for equilibrium states of quantum lattice systems with short-range interactions, to a large class of models possibly containing…

The century-long Michaelis-Menten rate law and its modifications in the modeling of biochemical rate processes stand on the assumption that the concentration of the complex of interacting molecules, at each moment, rapidly approaches an…

Computational feasibility of turbulent reacting flows hinges on the reduction of large chemical kinetics systems to smaller more manageable reaction sets. Recently, several sophisticated reduction techniques have been developed but they…

Stochastic models for biochemical reaction networks are widely used to explore their complex dynamics but face significant challenges, including difficulties in determining rate constants and high computational costs. To address these…

The application of the standard quasi-steady-state approximation to the Michaelis--Menten reaction mechanism is a textbook example of biochemical model reduction, derived using singular perturbation theory. However, determining the specific…

The classical approaches to the derivation of the (generalized) Mass Action Law (MAL) assume that the intermediate transition state (i) has short life time and (ii) is in partial equilibrium with the initial reagents of the elementary…

Using the prescription of the nonequilibrium statistical operator method, we derive a non-Markovian generalization to the kinetic theory described by Walser {\sl et al.} [Phys. Rev. A {\bf 59}, 3878 (1999)]. Quasi-particle damping and…

Reactions with enzymes are critical in biochemistry, where the enzymes act as catalysis in the process. One of the most used mechanisms for modeling enzyme-catalyzed reactions is the Michaelis-Menten (MM) kinetic. In the ODE level, i.e.…

The classic Michaelis-Menten equation describes the catalytic activities for ensembles of enzyme molecules very well. But recent single-molecule experiment showed that the waiting time distribution and other properties of single enzyme…

We distinguish a mechanical representation of the world in terms of point masses with positions and momenta and the chemical representation of the world in terms of populations of different individuals, each with intrinsic stochasticity,…

This paper studies a mathematical formalism of nonequilibrium thermodynamics for chemical reaction models with $N$ species, $M$ reactions, and general rate law. We establish a mathematical basis for J. W. Gibbs' macroscopic chemical…

In a conformational nonequilibrium steady state (cNESS), enzyme turnover is modulated by the underlying conformational dynamics. Based on a discrete kinetic network model, we use the integrated probability flux balance method to derive the…

It is well known in enzyme kinetics that the Michaelis-Menten (MM) equation is applicable only to enzymes in the steady state. We show that the result obtained in the previous work [Phys. Rev. Lett. 107, 218301 (2011)] is inconsistent with…

In this paper we prove that the well-known quasi-steady state approximations, commonly used in enzyme kinetics, which can be interpreted as the reduced system of a differential system depending on a perturbative parameter, according to…

The celebrated Michaelis-Menten (MM) expression provides a fundamental relation between the rate of enzyme catalysis and substrate concentration. The validity of this classical expression is, however, restricted to macroscopic amounts of…

The hypothesis of molecular chaos plays the central role in kinetic theory, which provides a closure leading to the Boltzmann equation for quantitative description of classic fluids. Yet how to properly extend it to active systems is still…

We introduce a reaction-path statistical mechanics formalism based on the principle of large deviations to quantify the kinetics of single-molecule enzymatic reaction processes under the Michaelis-Menten mechanism, which exemplifies an…