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Which of the listed effects would be brought about by any enzyme catalyzing the following simple reaction? $$\mathrm{S} \stackrel{k_{1}}{\rightleftharpoons_{k_{2}}} \mathrm{P} \quad \text { where } \quad K_{\mathrm{eq}}^{\prime}=\frac{[\mathrm{P}]}{[\mathrm{S}]}$$ (a) Decreased \(K_{\mathrm{eq}}^{\prime} ;\) (b) increased \(k_{1} ;\) (c) increased \(K_{\mathrm{eq}}^{\prime}\) (d) increased \(\Delta G^{\dagger} ;\) (e) decreased \(\Delta G^{\dagger} ;\) (f) more negative \(\Delta G^{\prime \circ}\) \((g)\) increased \(k_{2}\)

Short Answer

Expert verified
An enzyme would increase \(k_1\), \(k_2\), and decrease \(\Delta G^{\dagger}\).

Step by step solution

01

Understanding the Role of an Enzyme

Enzymes are biological catalysts that speed up the rate of a reaction without being consumed in the process. They work by lowering the activation energy of the reaction ( ΔG^{ is the activation energy) but do not influence the equilibrium constant ( K_{ which describes the ratio of the concentration of products to reactants in a reversible reaction.
02

Evaluating the Equilibrium Constant

Since enzymes do not alter the equilibrium constant of a reaction, options (a) "Decreased \(K_{\text{eq}}'\)" and (c) "Increased \(K_{\text{eq}}'\)" are incorrect. The equilibrium constant \(K_{\text{eq}}'\) is a ratio determined by the energies of the products and reactants, which remain unchanged by the presence of an enzyme.
03

Assessing Activation Energy Changes

Enzymes decrease the activation energy of reactions, which means that the energy required to initiate the transformation of reactants to products is lowered. Thus, option (e) "Decreased \(\Delta G^{\dagger}\)" is correct. In contrast, option (d) "Increased \(\Delta G^{\dagger}\)" is incorrect because it contradicts the role of enzymes.
04

Considering Reaction Rate Constants

Enzymes increase the reaction rate constants \(k_1\) and \(k_2\) because they make the transition state of the reaction more accessible. Therefore, options (b) "Increased \(k_1\)" and (g) "Increased \(k_2\)" are correct.
05

Evaluating Free Energy Change

The standard free energy change (G′°) of a reaction is also not influenced by the presence of an enzyme because it is determined by the nature of the reactants and products, not the pathway taken. Thus, option (f) "More negative \(\Delta G^{\prime \,\circ}\)" is incorrect.

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Key Concepts

These are the key concepts you need to understand to accurately answer the question.

Activation Energy
Activation energy is like the initial hurdle a reaction has to overcome to get started. For chemical reactions, this is the minimum energy required for reactants to transform into products. Think of it as the push needed to start a swing moving.
Enzymes play a crucial role in biochemical reactions by lowering this activation energy. They act like tiny machines that reduce the energy input required to reach the transition state, allowing the reaction to proceed faster.
Without altering the nature of the reactants or products, enzymes make it easier for a reaction to occur.
This is why in our original exercise, the correct choice included "Decreased \(\Delta G^{\dagger}\)". Enzymes decrease the activation energy, making them indispensable in biological systems where reactions need to happen rapidly and efficiently.
Equilibrium Constant
The equilibrium constant, often represented as \(K_{\text{eq}}\), provides insightful information about the ratio of product concentration to reactant concentration at equilibrium. It's an indicator of the position of equilibrium in a reversible reaction.
This constant is solely determined by the relationship of energies between reactants and products. Importantly, even though enzymes speed up the reaction rate, they don't alter the equilibrium constant itself.
This is because enzymes affect the path of the reaction rather than the final energy states of the substances involved.
  • Thus, whether an enzyme is present or not, the \(K_{\text{eq}}\) value remains unchanged.
  • This means options such as "Decreased \(K_{\mathrm{eq}}\)'" or "Increased \(K_{\mathrm{eq}}\)'" in the exercise are incorrect, because the enzyme does not impact the equilibrium position.
Reaction Rate
Reaction rate refers to how quickly a reaction proceeds. Enzymes play a vital role in increasing this rate by making it easier for reactants to achieve the transition state.
In simple terms, enzymes make performances run smoother and faster by optimizing conditions. This is achieved by reducing the barrier of activation energy, allowing more reactant molecules to convert into product molecules quickly.
Therefore, the steps in the original solution confirmed that options "Increased \(k_1\)" and "Increased \(k_2\)" were correct choices, as enzymes facilitate both forward and backward reactions due to this enhancement of reaction speed.
Free Energy Change
Free energy change, symbolized as \(\Delta G^{\prime \circ}\), is a measure of the Gibbs free energy difference between products and reactants under standard conditions. This value signifies the intrinsic stability and spontaneity of a reaction.
Notably, enzymes do not alter this free energy change.
  • The reaction's energy profile or the comparison between the start and end points stay as is. Enzymes just lower the activation barrier within these states.
  • Thus, claims that an enzyme could lead to a "More negative \(\Delta G^{\prime \circ}\)" would be inaccurate, reinforcing that enzymes only expedite reactions without shifting their inherent energy properties.
Hence, this reinforces that option "More negative \(\Delta G^{\prime \circ}\)" was indeed incorrect in the exercise. Enzymes influence the speed, not the free energy signature of a reaction.

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Most popular questions from this chapter

The enzyme urease enhances the rate of urea hydrolysis at pH 8.0 and \(20^{\circ} \mathrm{C}\) by a factor of \(10^{14}\). If a given quantity of urease can completely hydrolyze a given quantity of urea in 5.0 min at \(20^{\circ} \mathrm{C}\) and \(\mathrm{pH} 8.0,\) how long would it take for this amount of urea to be hydrolyzed under the same conditions in the absence of urease? Assume that both reactions take place in sterile systems so that bacteria cannot attack the urea.

An enzyme is found that catalyzes the reaction $$\mathrm{A} \rightleftharpoons \mathrm{B}$$ Researchers find that the \(K_{\mathrm{m}}\) for the substrate \(\mathrm{A}\) is \(4 \mu \mathrm{M},\) and the \(k_{\text {cat }}\) is \(20 \min ^{-1}\) (a) In an experiment, \([\mathrm{A}]=6 \mathrm{mM},\) and \(V_{0}=480 \mathrm{nM} \min ^{-1}\) What was the \(\left[\mathrm{E}_{\mathrm{t}}\right]\) used in the experiment? (b) In another experiment, \(\left[\mathrm{E}_{\mathrm{t}}\right]=0.5 \mu \mathrm{M},\) and the measured \(V_{0}=5 \mu \mathrm{M} \min ^{-1} .\) What was the \([\mathrm{A}]\) used in the experiment? (c) The compound \(\mathrm{Z}\) is found to be a very strong competitive inhibitor of the enzyme, with an \(\alpha\) of \(10 .\) In an experiment with the same \(\left[\mathrm{E}_{\mathrm{t}}\right]\) as in \((\mathrm{a}),\) but a different \([\mathrm{A}],\) an amount of \(\mathrm{Z}\) is added that reduces \(V_{0}\) to \(240 \mathrm{nM} \mathrm{min}^{-1}\). What is the \([\mathrm{A}]\) in this experiment? (d) Based on the kinetic parameters given above, has this enzyme evolved to achieve catalytic perfection? Explain your answer briefly, using the kinetic parameter(s) that define catalytic perfection.

The muscle enzyme lactate dehydrogenase catalyzes the reaction NADH and NAD' are the reduced and oxidized forms, respectively, of the coenzyme NAD. Solutions of NADH, but not \(\mathrm{NAD}^{+},\) absorb light at \(340 \mathrm{nm}\). This property is used to determine the concentration of NADH in solution by measuring spectrophotometrically the amount of light absorbed at \(340 \mathrm{nm}\) by the solution. Explain how these properties of NADH can be used to design a quantitative assay for lactate dehydrogenase.

Carbonic anhydrase of erythrocytes \(\left(M_{\mathrm{r}} 30,000\right)\) has one of the highest turnover numbers known. It catalyzes the reversible hydration of \(\mathrm{CO}_{2}\) : $$\mathrm{H}_{2} \mathrm{O}+\mathrm{CO}_{2} \rightleftharpoons \mathrm{H}_{2} \mathrm{CO}_{3}$$ This is an important process in the transport of \(\mathrm{CO}_{2}\) from the tissues to the lungs. If \(10.0 \mu g\) of pure carbonic anhydrase catalyzes the hydration of \(0.30 \mathrm{g}\) of \(\mathrm{CO}_{2}\) in \(1 \mathrm{min}\) at \(37^{\circ} \mathrm{C}\) at \(V_{\max },\) what is the turnover number \(\left(k_{\text {cat }}\right)\) of carbonic anhydrase (in units of \(\min ^{-1}\) )?

A research group discovers a new version of happyase, which they call happyase*, that catalyzes the chemical reaction $$\text { HAPPY } \rightleftharpoons \mathrm{SAD}$$ The researchers begin to characterize the enzyme. (a) In the first experiment, with \(\left[\mathrm{E}_{\mathrm{t}}\right]\) at \(4 \mathrm{n}\). , they find that the \(V_{\max }\) is \(1.6 \mu \mathrm{M} \mathrm{s}^{-1} .\) Based on this experiment, what is the \(k_{\text {cat }}\) for happyase \(^{*} ?\) (Include appropriate units.) (b) In another experiment, with \(\left[\mathrm{E}_{\mathrm{t}}\right]\) at \(1 \mathrm{nM}\) and [HAPPY] at \(30 \mu \mathrm{M}\), the researchers find that \(V_{0}=300 \mathrm{nM} \mathrm{s}^{-1}\). What is the measured \(K_{\mathrm{m}}\) of happyase \(^{*}\) for its substrate HAPPY? (Include appropriate units.) (c) Further research shows that the purified happyase used in the first two experiments was actually contaminated with a reversible inhibitor called ANGER. When ANGER is carefully removed from the happyase* preparation and the two experiments repeated, the measured \(V_{\max }\) in is increased to \(4.8 \mu \mathrm{M} \mathrm{s}^{-1},\) and the measured \(K_{\mathrm{m}}\) in (b) is now \(15 \mu\) M. For the inhibitor ANGER, calculate the values of \(\alpha\) and \(\alpha^{\prime}\) (d) Based on the information given above, what type of inhibitor is ANGER?

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