Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

What is Catalysis

Ask the average person in the street what a catalyst is, and he or she will probably tell you that a catalyst is what one has under the car to clean up the exhaust. Indeed, the automotive exhaust converter represents a very successful application of catalysis it does a great job in removing most of the pollutants from the exhaust leaving the engines of cars. However, catalysis has a much wider scope of application than abating pollution. [Pg.2]

Catalysts are the workhorses of chemical transformations in the industry. Approximately 85-90 % of the products of chemical industry are made in catalytic processes. Catalysts are indispensable in [Pg.2]

A catalyst offers an alternative, energetically favorable mechanism to the non-catalytic reaction, thus enabling processes to be carried out under industrially feasible conditions of pressure and temperature. [Pg.2]

For example, living matter relies on enzymes, which are the most specific catalysts one can think of. Also, the chemical industry cannot exist without catalysis, which is an indispensable tool in the production of bulk chemicals, fine chemicals and fuels. [Pg.2]

For scientists and engineers catalysis is a tremendously challenging, highly multidisciplinary field. Let us first see what catalysis is, and then why it is so important for mankind. [Pg.2]


What is the scope of Lewis-acid catalysis of Diels-Alder reactions in water An approach of extending the scope by making use of a temporary secondary coordination site is described in Chapter 4. [Pg.32]

What is the effect of micelles on the aqueous Diels-Alder reaction Can micellar catalysis be combined with Lewis-acid catalysis In Chapter 5 these aspects will discussed. [Pg.32]

For what is probably the earliest microscopic calculations of thermodynamic cycles in proteins see Ref. 12, that reported a PDLD study of the pKtt s of some groups in lysozyme. The use of FEP approaches for studies of proteins is more recent and early studies of catalysis and binding were reported in Refs. 11, 12, and 13 of Chapter 4. [Pg.186]

The HIV-1 protease, like other retroviral proteases, is a homodimeric aspartyl protease (see Fig. 1). The active site is formed at the dimer interface, with the two aspartic acids located at the base of the active site. The enzymatic mechanism is thought to be a classic acid-base catalysis involving a water molecule and what is called a push-pull mechanism. The water molecule is thought to transfer a proton to the dyad of the carboxyl groups of the aspartic acids, and then a proton from the dyad is transferred to the peptide bond that is being cleaved. In this mechanism, a tetrahedral intermediate transiently exists, which is nonconvalent and which is mimicked in most of the currently used FDA approved inhibitors. [Pg.87]

Zeolite Membranes in Catalysis What Is New and How Bright Is the Future ... [Pg.211]

Explain the concepts of atom efficiency and environmental friendliness. What is an E-factor Which processes usually have the highest E-factors Explain what catalysis means on the different length scales indicated in Eig. 1.8. [Pg.401]

What is the aim of reaction rate theory Is the theory of practical use for scientists working in catalysis ... [Pg.403]

We have just discussed several common strategies that enzymes can use to stabilize the transition state of chemical reactions. These strategies are most often used in concert with one another to lead to optimal stabilization of the binary enzyme-transition state complex. What is most critical to our discussion is the fact that the structures of enzyme active sites have evolved to best stabilize the reaction transition state over other structural forms of the reactant and product molecules. That is, the active-site structure (in terms of shape and electronics) is most complementary to the structure of the substrate in its transition state, as opposed to its ground state structure. One would thus expect that enzyme active sites would bind substrate transition state species with much greater affinity than the ground state substrate molecule. This expectation is consistent with transition state theory as applied to enzymatic catalysis. [Pg.32]


See other pages where What is Catalysis is mentioned: [Pg.3]    [Pg.4]    [Pg.10]    [Pg.11]    [Pg.13]    [Pg.15]    [Pg.17]    [Pg.21]    [Pg.3]    [Pg.4]    [Pg.10]    [Pg.11]    [Pg.13]    [Pg.15]    [Pg.17]    [Pg.21]    [Pg.193]    [Pg.2]    [Pg.239]    [Pg.224]    [Pg.220]    [Pg.222]    [Pg.228]    [Pg.234]    [Pg.390]    [Pg.19]    [Pg.401]    [Pg.304]    [Pg.8]    [Pg.53]    [Pg.3]    [Pg.73]    [Pg.250]    [Pg.361]    [Pg.387]    [Pg.379]    [Pg.616]    [Pg.164]    [Pg.458]    [Pg.56]   


SEARCH



What is

© 2024 chempedia.info