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Transition state of a reaction

Orbital-based methods can be used to compute transition structures. When a negative frequency is computed, it indicates that the geometry of the molecule corresponds to a maximum of potential energy with respect to the positions of the nuclei. The transition state of a reaction is characterized by having one negative frequency. Structures with two negative frequencies are called second-order saddle points. These structures have little relevance to chemistry since it is extremely unlikely that the molecule will be found with that structure. [Pg.94]

Any discussion based on reactivity ratios is kinetic in origin and therefore reflects the mechanism or, more specifically, the transition state of a reaction The transition state for the addition of a vinyl monomer to a growing radical involves the formation of a partial bond between the two species, with a corre sponding reduction of the double-bond character of the vinyl group in the monomer ... [Pg.436]

The value of is the difference in partial molal volume between the transition state and the initial state, but it can be approximated by the molar volume. Increasing pressure decreases the value of AV and if A V is negative the reaction rate is accelerated. This equation is not strictly obeyed above lOkbar. If the transition state of a reaction involves bond formation, concentration of charge, or ionization, a negative volume of activation often results. Cleavage of a bond, dispersal of charge, neutralization of the transition state and diffusion control lead to a positive volume of activation. Reactions for which rate enhancement is expected at high pressure include ... [Pg.457]

The possible mechanisms for solvolysis of phosphoric monoesters show that the pathway followed depends upon a variety of factors, such as substituents, solvent, pH value, presence of nucleophiles, etc. The possible occurrence of monomeric metaphosphate ion cannot therefore be generalized and frequently cannot be predicted. It must be established in each individual case by a sum of kinetic and thermodynamic arguments since the product pattern frequently fails to provide unequivocal evidence for its intermediacy. The question of how free the PO ion actually exists in solution generally remains unanswered. There are no hard boundaries between solvation by solvent, complex formation with very weak nucleophiles such as dioxane or possibly acetonitrile, existence in a transition state of a reaction, such as in 129, or SN2(P) or oxyphosphorane mechanisms with suitable nucleophiles. [Pg.102]

The transition state of a reaction bears greater resemblance to the less stable species (of reactant or reaction intermediate or product). See Hammond Postulate... [Pg.418]

The point of minimal potential energy in the trajectory of reactants to products in a chemical reaction. A reaction s saddle point (or coF) indicates the geometry and energy of reactants as they approach and pass the transition state of a reaction. [Pg.625]

The transition state of a reaction is difficult to study because it is so short-lived. To understand enzymatic catalysis, however, we must dissect the interaction between the enzyme and this ephemeral moment in the course of a reaction. Complementarity between an enzyme and the transition state is virtually a requirement for catalysis, because the energy hill upon which the transition state sits is what the enzyme must lower if catalysis is to occur. How can we obtain evidence for enzyme-transition state complementarity Fortunately, we have a variety of approaches, old and new, to address this problem, each providing compelling evidence in support of this general principle of enzyme action. [Pg.220]

It is not easy to design an experiment to test the subtle stereochemical requirement of the transition state of a reaction. One experimental approach is to attach the nucleophile to the substrate, creating a situation where this nucleophile can undergo two different competing reactions. In many cases, the nucleophile can more easily fulfill the stereochemical requirement of one process and only one reaction is observed. The experiment is almost perfectly designed when the process which takes place is "stereoelec-tronically allowed" and leads to the kinetic rather than the thermodynamic product, or when the process which does not take place is not "stereoelec-tronically allowed" but is otherwise favored on the basis of steric arguments or entropy consideration, especially when that would have led to the thermodynamic product. [Pg.90]

The effect of micelles on organic reactions can be attributed to both electrostatic and hydrophobic interactions (Rosen, 1979). Electrostatic interaction is important because it may affect the transition state of a reaction orthe concentration of reactant in the vicinity ofthe reaction site. The hydrophobic interactions are important because they determine the extent and the locus of solubilization in the micelle. [Pg.83]

Building on an idea of Haldane (Chapter 5) advanced in the 1920s, in 1944 Pauling and Pressmann formulated the hypothesis of complementarity of the catalyst with the transition state of a reaction. Until then it was assumed that the ground state of a substrate was bound most tightly to the enzyme molecule. [Pg.512]

The idea that antibodies also can stabilize the transition state of a reaction, that they feature a sterically or electronically complementary active center to the ratedetermining transition state just like enzymes, has existed since 1969. This concept of catalytic antibodies could be investigated only after the advent of monoclonal antibodies. The capability to raise molecularly uniform antibodies instead of polyclonal sera... [Pg.514]

Explain how the transition state of a reaction can be used to design an enzyme inhibitor. [Pg.158]

Equation 15.1 offers a quantitative formulation of this statement. This equation makes a statement about the stabilization AEJS of the transition state of a reaction between substrate I (reacting at its reactive center 1, where its frontier orbitals have the coefficients Cj HOMOl and C i LUMOj) and substrate II (reacting at its reactive center 1 as well, where its frontier orbitals have the coefficients C] H0M0[l and Cj LUMOn) owing to the two frontier orbital interactions ... [Pg.650]

The range of enzyme function can be condensed into catalytic task space, where each point represents a catalytic task and an enzyme covers a portion of the space corresponding to its repertoire of functions (Kauffman, 1992 Kauffman, 1993). In addition to the shape features, the axes include chemical and physical aspects relevant to catalysis. This construction of catalytic space was motivated by the discovery of antibody catalysis through binding of the transition state of a reaction (Lienhrd,... [Pg.147]

We are often interested in the activated complex or transition state of a reaction—that is, the halfway point beyond which the system becomes more likely to progress to the products than return to the reactants. Similarly important are the reaction intermediates, species formed during the course of the reaction, which exist for a significant time interval, but which are ultimately consumed. Reaction intermediates often may be detected physically or chemically. Of the many methods for studying reaction mechanisms, the most important is the determination of the rate law, the quantitative relationship between the reaction speed at a fixed temperature and the concentrations of the reagents. The rate law will often indicate the species that participate in the ratedetermining step of the reaction. [Pg.365]

Gibbs energy of activation A G (standard free energy of activation A G ) (Id mol-1) — The standard Gibbs energy difference between the -> transition state of a reaction (either an elementary reaction or a stepwise reaction) and the ground state of the reactants. It is calculated from the experimental rate constant k via the conventional form of the absolute reaction rate equation ... [Pg.304]

According to the Hammond postulate, the transition state of a reaction resembles the structure of the species (reactant or product) to which it is closer in energy. A transition state is always higher in energy than both the reactants and products, so it will resemble the structure of either the reactant or product, whichever is higher in energy. [Pg.260]

It has already been reported that antibodies prepared against the transition state of a reaction show considerable catalytic activity [113]. For example, antibodies prepared against a phosphonic ester (as a transition state analogue for alkaline ester hydrolysis) enhanced the rate of ester hydrolysis by 10 -10" fold. Recently, similar systems based on imprinted polymers which display high catalytic activity have been successfully prepared. Initial attempts were performed by several groups [114-117] with imprinted polymers based on non-stoichiometric, non-covalent interactions, which, however, gave results far below those obtained with antibodies. Rate enhancements up to 6.7-fold were reached in one case. [Pg.102]

The free energy relationships involving concentration variables differ from the normal ones in that they give information only about stoichiometry and not about the charge structure of the transition state of a reaction. The topic is very extensive and for this reason we refer the reader to more advanced texts and references for further information. [Pg.43]


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See also in sourсe #XX -- [ Pg.7 , Pg.20 ]




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