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UW-Madison CHEM 104 - Enzymes
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CHEM 104 1st Edition Lecture 18Enzymes continued: • General mechanism: (first step is fast, second is slow) Step 1) E(enzyme) + S(substrate)  ES(enzyme-substrate complex)Step 2) ES  P(product) + E• Enzymes lowers activation energy by changing mechanism • Enzymes can become inactive if they are denatured, or if they are inhibited• Example: lysozyme is enzyme that catalyzes the hydrolysis of polysaccharides that form bacterial cell wallsCharacteristics of chemical equilibrium• At equilibrium, both reactants and products are present and the concentrations of all species areconstant• Equilibrium is independent of directiono For a specific reaction at a given temperature, the equilibrium state is the same no matter what the direction of approach to equilibrium • The equilibrium concentrations are not changed by a catalyst – but equilibrium is reached faster since a catalyst speeds up both forward and reverse reactions • Equilibrium is dynamico At equilibrium, rate1 = rate-1• There is a mathematical relationship between equilibrium concentrationso aA + bB  cC + dDEquilibrium constant Kc = [C]c[D]d/[A]a[B]bThese notes represent a detailed interpretation of the professor’s lecture. GradeBuddy is best used as a supplement to your own notes, not as a substitute.o Heterogeneous equilibrium: include in the expression of kc only concentrations that will change (i.e. gases and dilute aqueous


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