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Chapter 24
Catalysis

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24-01b
Title
Figure 24.1(b)
Caption
Reaction coordinate diagrams for catalyzed vs. uncatalyzed reaction.
Notes
This figure shows the case where catalysis occurs because the catalyst lowers the energy of the transition state without changing the reaction mechanism.
Keywords
figure, 24.1(b) , reaction coordinate, diagrams, catalyzed, uncatalyzed
24-02
Title
Figure 24.2
Caption
Reaction coordinate diagrams for catalyzed vs. uncatalyzed reaction involving change of mechanism.
Notes
This figure shows the case where catalysis occurs because the catalyst lowers the energy of the activated complex by changing the reaction mechanism.
Keywords
figure, 24.2 , reaction coordinate, diagrams, catalyzed, uncatalyzed, change, mechanism
24-03a,b
Title
Figure 24.3
Caption
Reaction coordinate diagrams for specific-acid-catalyzed and general-acid-catalyzed reactions.
Notes
In specific-acid catalysis proton transfer leads to an intermediate preceding the rate-determining step. In general-acid catalysis proton transfer occurs during the rate-determining step
Keywords
figure, 24.3, reaction coordinate, diagrams, specific-acid-catalyzed, general-acid-catalyzed
24-03-31UNa,b
Title
Lock-and-Key vs. Induced-Fit Models
Caption
Schematic diagram illustrating the difference between the lock-and-key and induced-fit models of enzyme catalysis.
Notes
In the lock-and-key model the enzyme active site does not change its shape to accommodate the substrate, whereas in the induced-fit model this does occur.
Keywords
lock-and-key, induced-fit, enzyme, catalysis
24-06
Title
Top Half of Figure 24.6
Caption
Schematic diagram illustrating shapes and polarities of the binding pockets of trypsin, chymotrypsin, and elastase.
Notes
Shapes and charge distributions in binding pockets explain why trypsin binds long basic (cationic) amino acids, chymotrypsin binds flat, nonpolar amino acids, and elastase binds only small amino acids.
Keywords
figure, 24.6, binding, pockets, trypsin, chymotrypsin, elastase
24-10
Title
Figure 24.10
Caption
pH-Rate Profile for Lysozyme.
Notes
The optimum pH for enzyme activity is the pH midway between the pKa of a basic group which needs to be in its basic form to be active and an acidic group which needs to be in its acid form to be active.
Keywords
figure, 24.10, pH-rate, profile, lysozyme
24-11
Title
Figure 24.11
Caption
Proposed mehanism of isomerization of d-glucose-6-phosphate to d-fructose-6-phosphate.
Notes
This mechanism involves ring opening, three tautomerization steps which shift the carbonyl by one carbon, and ring closure.
Keywords
figure, 24.11, mechanism, isomerization, d-glucose-6-phosphate, d-fructose-6-phosphate

Title
Table 24.1 The pKa of Metal-Bound Water
Caption
Notes
Keywords

Title
Table 24.2 Relative Rates of an Intermolecular Reaction and Five Intramolecular Reactions
Caption
Notes
Keywords

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