Biochemical reactions reaction plots

PLOTS OF THERMODYNAMIC PROPERTIES OF BIOCHEMICAL REACTIONS VERSUS pH... 

Plots of Thermodynamic Properties of Biochemical Reactions versus pH... 

Plot the change in binding of hydrogen ions versus pH at ionic strength 0.25 M for the following five biochemical reactions ... 

Consider the biochemical reaction mechanism shown in fig. 4.8, which occurs in glycolysis [7] note the similarity in the structure of this mechanism to that of a model of a chemical neuron shown in fig. 4.1. Calculations of the stable stationary states of the biochemical system of fig. 4.8 are plotted in fig. 4.9. The change from high to low concentration of either compound is not as abrupt as that in fig. 4.2 for the chemical model, but is clearly present. We have identified a computational element, a fuzzy chemical neuron, in a biochemical reaction. 

A double reciprocal plot of kinetic data for a biochemical reaction that obeys a Monod rate law will yield a value of Pmax from the reciprocal of the intercept of the y-axis. The corresponding slope is equal to At high val-... 

Figure 113.6 contains a plot of rate versus cell concentration for an autocatalytic biochemical reaction whose rate law is of the logistic form... 

Figure 9 The effect of pH on kj and k i for the binding of to pyrene-iabeiied recombinant inositol monophosphatase. Enzyme (3 (jlm final concentration) was reacted with various concentrations of Mg " ions in 50 mw Tris-HCI buffer at pH 9.0 ( ), pH 8.0 ), pH 7.3 ) and pH 6.5 (O) at 20°C. The for each reaction is plotted against the final concentration of ions used. Reproduced with permission from Thorne, M. R., Greasiey, P. J. and Gore, M. G. (1996) BiochemicalJoumal, 315, 989-994. Biochemical Society.

I ig 5-Extent of the reaction between iodoinsulins and sulphite. The time course of the reaction at pH 7 and 37 0 was determined as shown in fig. 1 and the maximum extent of the reaction plotted against the iodina-tion degree (from Rosa et al., Biochem. J., 103. 407, 1967). 

Fig. 20. Plots of standard Gibbs free energies for dehydrogenation reactions of formate [reaction (32)], acetate [reaction (33)], and propanoate [reaction (34)] as functions of temperature at Values of used in biochemical reaction networks are also shown (see text)...

Figure 9.3 Plot of the base 10 logarithm of the apparent equilibrium constant K for the nitrogen fixation reaction (see reaction 9.5-2) versus pH at 298.15 K (see Problem 9.2). [With permission from R. A. Alberty, Arch. Biochem. Biophys. 389, 94-109 (2001). Copyright Academic Press.]...

These last two plots have shown the importance of determinations of acid dissociation constants of biochemical reactants. In the next chapter we will see that it is also important to know the pKs of acid groups when heats of reaction are determined calorimetrically. 

Although these reactions are complex at a biochemical level, their kinetics approximate to reactions of the first order. Thus, the kinetics of inactivation of populations of pure cultures of micro-organisms take the typical exponential form of reactions of the first order. What this means in experimental practice is that there is a linear relationship when numbers of microorganisms held at high temperatures are plotted on a logarithmic scale against time plotted on an arithmetic scale (Fig. 1). 

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