Catalyst is a compound that by its addition to a reaction increases



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Chapter 23: Catalysis 21-1

Catalyst and Catalysis: Introduction Catalyst is a compound that by its addition to a reaction increases the rate of the reaction without itself being consumed or changed at the end of the reaction (cycle). The reaction is then called being catalyzed. The phenomenon of catalyst in accelerating reaction is called catalysis. HN O Ph 3 PAuNTf 2 (5 mol %) MsOH (1.2 equiv), 4 Å MS CH 2 Cl 2 quantitative (NMR)/ 61% (isolated) N O H + Ph 3 PAu + HN O AuPPh 3 HN O Au H + HN O Ph 3 PAu + MsO PPh 3 23-2

Catalyst and Catalysis: Introduction Catalyst increases the reaction rate by providing a pathway with lower free energy of activation (reaction kinetics) 23-3

Catalysis in Organic Reactions In organic reactions, several ways to accelerate reactions by catalysts: Increase electrophilicity Increase nucleophilicity Increase leaving ability as a nucleofuge (decrease electrophilicity) Increase the stability of a transition state Four types of catalysis: acid catalysis base catalysis nucleophilic catalysis metal-ion catalysis 23-4

Acid Catalysis: Ester Hydrolysis 23-5

Acid Catalysis Specific-acid catalysis and general acid catalysis Specific-acid catalysis: proton is fully transferred before the slow step of the reaction (typically strong acidic conditions, two-stages) General acid catalysis: proton transfer to the reactant during the slow step of the reaction (typically under weak acidic conditions, one stage) 23-6

Acid Catalysis General-acid catalysis vs. specific-acid catalysis 23-7

Base Catalysis General-base catalysis vs. specific-base catalysis 23-8

Nucleophilic Catalysis The catalyst is nucleophile and forms a covalent bond with reactants/intermediates Also called covalent catalysis 23-9

tal-ion Catalysis Lewis acid catalysis (metal ions are Lewis acids) 23-10

tal-ion Catalysis Examples: 23-11

tal-ion Catalysis 23-12

Intramolecular Reactions 1000 times faster Effective molarity (EM) is the concentration of the reactant that would be required in an intermolecular reaction for it to achieve the same rate as intramolecular reaction 23-13

Intramolecular Reactions R =, EM = 2.3 x 10 4 M R = ipr, EM = 1.3 x 10 6 M EM = 2.2x10 5 M EM = 1 x 10 7 M 23-14

Intramolecular Catalysis A catalyst is embedded or covalently bonded to substrates Also called anchimeric effect/assistance Due to intramolecularity, the catalysis should be more efficient. 70000 times Faster in the Trans isomer 23-15

Intramolecular Catalysis: Example 23-16

Intramolecular Catalysis: Example 23-17

Catalysis in Biological Reactions Most biological catalysts are enzymes (belongs to globular proteins) Substrates and active sites (where the reaction occurs) Substrates bound to the active site Specificity (molecular recognition) Lock-and-key model Induced-fit model Hexokinase Red: before binding Blue: after binding 23-18

Enzyme Catalysis How do enzymes do catalysis? Reacting groups are brought together in a proper orientation Some of the amino acid side chains as well as bounded metal ions as catalyst Stabilizing the transition states and intermediates via van der Waals interactions, electrostatic interactions, and H-bonding. Naming of enzymes End typically with ase, indicating breaking the bond Peptidase: breaking the peptide bond Esterase: breaking the ester bond Synthase Synthesizing instead of breaking it down. 23-19

Carboxypeptidase A talloenzyme (enzymes containing tightly bound metal ions) Hydrolyze C-terminal except lysine and arginine. 23-2020

Serine Proteases Trypsin, chymotrypsin and elastase are members of endopeptidases known as serine proteases 23-2121

Serine Proteases Proposed mechanism for chymotrypsin- catalyzed hydrolysis 23-2222

Lysozyme Catalyze the hydrolysis of the bacterial cell wall NAM-NAG bond (NAM: N-Acetylmuramic acid) 23-23

Protein ph-rate Profile lysozyme The phs at which the enzyme are 50% active corresponds to the pka of enzyme s catalytic groups (as long as those values are at lease 2 units apart. Why pka of Asp52 is 3.8 but pka of Glu35 is 6.7 instead of 4.25 in its free form? 23-2424

Glucose-6-Phosphate Isomerase 23-2525

Aldolase 23-2626