Premise Photosynthetic light-response (PLR) curves for leaves are important components of models related to carbon fixation in forest ecosystems, linking the Mitscherlich equation and Michaelis–Menten traits leaf economics spectrum (LES). However, do not consider changes habits (i.e., evergreen deciduous) within-canopy shading variation these PLR curves. Methods Here, we measured sun shade 44 3...

In most of the real life problems, we encounter with nonlinear differential equations. Problems are made more understandable by modeling them these this way, it becomes easier to interpret problems and reach results. 1913, basic enzymatic reaction model introduced Michaelis Menten describe enzyme processes is an example equation. This one simplest best-known approaches mechanisms used enzyme-ca...

where K and V are some unknowns. For example, in study of chemical reactions, equation (1.1) is known as the Michaelis–Menten equation which describes the theoretical interrelation between the speed of reaction v(s) and the amount of reagent s. In this case the parameter V has the meaning of a maximally possible speed of reaction and the parameter K is the value of s for which the speed of reac...

This paper summarizes our present theoretical understanding of single-molecule kinetics associated with the Michaelis-Menten mechanism of enzymatic reactions. Single-molecule enzymatic turnover experiments typically measure the probability density f(t) of the stochastic waiting time t for individual turnovers. While f(t) can be reconciled with ensemble kinetics, it contains more information tha...

Nearly 100 years ago Michaelis and Menten published their now classic paper [Michaelis, L., and Menten, M. L. (1913) Die Kinetik der Invertinwirkung. Biochem. Z. 49, 333-369] in which they showed that the rate of an enzyme-catalyzed reaction is proportional to the concentration of the enzyme-substrate complex predicted by the Michaelis-Menten equation. Because the original text was written in G...

Many enzymatic reactions in biochemistry are far more complex than the celebrated Michaelis-Menten scheme, but the observed turnover rate often obeys the hyperbolic dependence on the substrate concentration, a relation established almost a century ago for the simple Michaelis-Menten mechanism. To resolve the longstanding puzzle, we apply the flux balance method to predict the functional form of...

Recent fluorescence spectroscopy measurements of single-enzyme kinetics have shown that enzymatic turnovers form a renewal stochastic process in which the inverse of the mean waiting time between turnovers follows the Michaelis-Menten equation. We study enzyme kinetics at physiologically relevant mesoscopic concentrations using a master equation. From the exact solution of the master equation w...

Enzymes are dynamic entities: both their conformation and catalytic activity fluctuate over time. When such fluctuations are relatively fast, it is not surprising that the classical Michaelis-Menten (MM) relationship between the steady-state enzymatic velocity and the substrate concentration still holds. However, recent single-molecule experiments have shown that this is the case even for an en...