Lecture 15 Chemical Reaction Engineering (CRE) is the field that studies the rates and mechanisms of chemical reactions and the design of the reactors.

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Lecture 15 Chemical Reaction Engineering (CRE) is the field that studies the rates and mechanisms of chemical reactions and the design of the reactors in which they take place.

Lecture 15 – Thursday 2/24/2011 Enzymes Michealis-Menten Kinetics Lineweaver-Burk Plot Enzyme Inhibition Competitive Uncompetitive

Last Lecture

Last Lecture 1.In the PSSH, we set the rate of formation of the active intermediates equal to zero. If the active intermediate A* is involved in m different reactions, we set it to: 2. The azomethane (AZO) decomposition mechanism is By applying the PSSH to AZO*, we show the rate law, which exhibits first-order dependence with respect to AZO at high AZO concentrations and second- order dependence with respect to AZO at low AZO concentrations.

Enzymes Michaelis-Menten Kinetics. Enzymes are protein like substances with catalytic properties. Enzyme unease. [From Biochemistry, 3/E by Stryer, copywrited 1988 by Lubert Stryer. Used with permission of W.H. Freeman and Company.]

Enzymes It provides a pathway for the substrate to proceed at a faster rate. The substrate, S, reacts to form a product P. Slow S P Fast A given enzyme can only catalyze only one reaction. Example, Urea is decomposed by the enzyme urease.

A given enzyme can only catalyze only one reaction A given enzyme can only catalyze only one reaction. Urea is decomposed by the enzyme urease, as shown below. The corresponding mechanism is:

Michaelis-Menten Kinetics

Michaelis-Menten Kinetics

Vmax=kcatEt Turnover Number: kcat Number of substrate molecules (moles) converted to product in a given time (s) on a single enzyme molecule (molecules/molecule/time) For the reaction H2O2 + E →H2O + O + E kcat 40,000,000 molecules of H2O2 converted to product per second on a single enzyme molecule.

-rs CS (Michaelis-Menten plot) Vmax Solving: KM=S1/2 Michaelis-Menten Equation (Michaelis-Menten plot) Vmax -rs S1/2 Solving: KM=S1/2 therefore KM is the concentration at which the rate is half the maximum rate CS

Inverting yields Lineweaver-Burk Plot slope = KM/Vmax 1/Vmax 1/S 1/-rS

Types of Enzyme Inhibition Competitive Uncompetitive Non-competitive

Competitive Inhibition

Competitive Inhibition 1) Mechanisms:

Competitive Inhibition 2) Rates:

Competitive Inhibition

Competitive Inhibition From before (no competition): No Inhibition Competitive Increasing CI Competitive Intercept does not change, slope increases as inhibitor concentration increases

Uncompetitive Inhibition Inhibition only has affinity for enzyme-substrate complex Developing the rate law (1) (2)

Adding (1) and (2) From (2)

Total enzyme

Slope remains the same but intercept changes as inhibitor concentration is increased Lineweaver-Burk Plot for uncompetitive inhibition

Non-competitive Inhibition (Mixed) E + S E·S P + E (inactive)I.E + S I.E.S (inactive) +I -I Both slope and intercept changes Increasing I No Inhibition

End of Lecture 15