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State specific rate constant relation

A. Precision of Specific Rate Constants. For a simple reaction system of a given order, the rate constant may be calculated from data giving the state of the system at two different times. This assumes that sufficient measurements have been made to establish the order of the reaction so that the functional relation is known. [Pg.86]

These reactions are modelled in terms of a diffusional step or kd[ff), resulting in the formation of a bimolecular encounter complex. This is followed by competing pathways for dissociation of the complex or or energy transfer k or k ). Deactivation of the excited quencher is described by p. The observed CPL is directly proportional to the difference in excited state concentrations of the two enantiomers, and this may be related to the specific rate constants introduced above. If, for example, we make the reasonable assumption that the diffusion and deactivation are independent of chirality, one can derive the following expression for AN t)... [Pg.250]

Note that the sums are restricted to the portion of the frill S matrix that describes reaction (or the specific reactive process that is of interest). It is clear from this definition that the CRP is a highly averaged property where there is no infomiation about individual quantum states, so it is of interest to develop methods that detemiine this probability directly from the Scln-ddinger equation rather than indirectly from the scattering matrix. In this section we first show how the CRP is related to the physically measurable rate constant, and then we discuss some rigorous and approximate methods for directly detennining the CRP. Much of this discussion is adapted from Miller and coworkers [44, 45]. [Pg.990]

Each enzyme has a working name, a specific name in relation to the enzyme action and a code of four numbers the first indicates the type of catalysed reaction the second and third, the sub- and sub-subclass of reaction and the fourth indentifies the enzyme [18]. In all relevant studies, it is necessary to state the source of the enzyme, the physical state of drying (lyophilized or air-dried), the purity and the catalytic activity. The main parameter, from an analytical viewpoint is the catalytic activity which is expressed in the enzyme Unit (U) or in katal. One U corresponds to the amount of enzyme that catalyzes the conversion of one micromole of substrate per minute whereas one katal (SI unit) is the amount of enzyme that converts 1 mole of substrate per second. The activity of the enzyme toward a specific reaction is evaluated by the rate of the catalytic reaction using the Michaelis-Menten equation V0 = Vmax[S]/([S] + kM) where V0 is the initial rate of the reaction, defined as the activity Vmax is the maximum rate, [S] the concentration of substrate and KM the Michaelis constant which give the relative enzyme-substrate affinity. [Pg.445]

The calculation of rate constants from steady state kinetics and the determination of binding stoichiometries requires a knowledge of the concentration of active sites in the enzyme. It is not sufficient to calculate this specific concentration value from the relative molecular mass of the protein and its concentration, since isolated enzymes are not always 100% pure. This problem has been overcome by the introduction of the technique of active-site titration, a combination of steady state and pre-steady state kinetics whereby the concentration of active enzyme is related to an initial burst of product formation. This type of situation occurs when an enzyme-bound intermediate accumulates during the reaction. The first mole of substrate rapidly reacts with the enzyme to form stoichiometric amounts of the enzyme-bound intermediate and product, but then the subsequent reaction is slow since it depends on the slow breakdown of the intermediate to release free enzyme. [Pg.415]

In summary, it can be seen for the three-step reaction scheme of this example that the net rate of the overall reaction is controlled by three kinetic parameters, KTSi, that depend only on the properties of the transition states for the elementary steps relative to the reactants (and possibly the products) of the overall reaction. The reaction scheme is represented by six individual rate constants /c, and /c the product of which must give the equilibrium constant for the overall reaction. However, it is not necessary to determine values for five linearly independent rate constants to determine the rate of the overall reaction. We conclude that the maximum number of kinetic parameters needed to determine the net rate of overall reaction is equal to the number of transition states in the reaction scheme (equal to three in the current case) since each kinetic parameter is related to a quasi-equilibrium constant for the formation of each transition state from the reactants and/or products of the overall reaction. To calculate rates of heterogeneous catalytic reactions, an addition kinetic parameter is required for each surface species that is abundant on the catalyst surface. Specifically, the net rate of the overall reaction is determined by the intrinsic kinetic parameters Kf s as well as by the fraction of the surface sites, 0, available for formation of the transition states furthermore, the value of o. is determined by the extent of site blocking by abundant surface species. [Pg.181]

Increased attention has been focused on vibrational, rotational, and translational nonequilibria in reacting systems as well. To account for these nonequilibrium effects, it is becoming increasingly traditional to express specific reaction-rate constants in terms of sums or integrals of reaction cross-sections over states or energy levels of the reactants involved [3], [11]. This approach helps to relate the microscopic and macroscopic aspects of rate processes and facilitates the use of fundamental experimental information, such as that obtained from molecular-beam studies [57], in calculation of macroscopic rate constants. Proceeding from measurements at the molecular level to obtain the rate constant defined in equation (4) remains a large and ambitious task. [Pg.594]

Equation 4 clearly shows how, for this specific mechanism, the rate constants are related to the steady state coefficients (< >) in Equation 2. The glucose oxidase mechanism (see below) is a special case of equations 3 and 4. [Pg.309]

Naively, one would expect that solvolysis rates constants, and ig, in solvents Si and S2 would be related as in (16). This would not be the case however, if one of the solvents were specifically involved in the transition state, i.e. if the solvolysis were not a pure S l process, but depended on solvent nucleophilicity (Winstein et ah, 1965). [Pg.183]

Encounter of excited sensitizer with the electron relay leads to the formation of a precursor complex. The electron transfer event occurs within this pair to yield a successor complex. The latter subsequently dissociates into free product ions or reacts back to the starting material. When the stationary state approximation is used the observed (bimolecular) rate constant for product formation can be related to the specific rates of the individual steps in Scheme I by ... [Pg.52]


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See also in sourсe #XX -- [ Pg.299 ]




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