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Chapter 20: Problem 5

A wealthy investor has come to you for advice. She has been approached by a biochemist who seeks financial backing for a company that would market dinitrophenol and dicumarol as weight-loss medications. The biochemist has explained to her that these agents are uncouplers and that they would dissipate metabolic energy as heat. The investor wants to know if you think she should invest in the biochemist's company. How do you respond?

Short Answer

Expert verified
Considering the potentially dangerous effects of dinitrophenol and dicumarol, it would be advisable not to invest in the proposed company.

Step by step solution

01

Understanding Dinitrophenol and Dicumarol

Dinitrophenol and dicumarol are uncoupling agents known in biochemical fields. They work by making the inner mitochondrial membrane porous. This leads to proton leakage, effectively skipping ATP synthesis. As a result, the energy from glucose oxidation is released as heat.
02

Analyzing the Effects of Dispensing Metabolic Energy as Heat

Increasing the body's heat generation process can theoretically lead to weight loss, as it increases the body's metabolic rate. This means the body uses more energy, potentially leading to fat loss. However, this usually comes at the expense of excessive heat and potential body damage. It's important to consider the associated health risks.
03

Evaluate the Risks and the Benefits

Both substances were used in the past for weight loss. However, they often resulted in harmful side effects, such as hyperthermia. Dinitrophenol especially is known to have a narrow therapeutic window, which makes it dangerous. Today, their use is generally discouraged due to these adverse effects. Therefore, while the weight loss theory is scientifically plausible, it might not be ethically justified considering the potential health risks.
04

Presenting the Final Advice

With the scientific, ethical and financial aspects taken into consideration, the advisability in this case would be not to invest in the biochemist's company. The risks associated with these agents, and the potential legal and ethical issues that might arise from their side effects, make this investment opportunity unappealing.

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Most popular questions from this chapter

The standard reduction potential for (NAD \(^{+} / \mathrm{NADH}\) ) is \(-0.320 \mathrm{V}\) and the standard reduction potential for (pyruvate/lactate) is \(-0.185 \mathrm{V}\) a. What is the standard free energy change \(\left(\Delta G^{\circ \prime}\right)\) for the lactate dehydrogenase reaction: \\[ \mathrm{NADH}+\mathrm{H}^{+}+\text {pyruvate } \longrightarrow \text { lactate }+\mathrm{NAD}^{+} \\] b. What is the equilibrium constant \(\left(K_{\mathrm{eq}}\right)\) for this reaction? c. If [pyruvate] \(=0.05 \mathrm{m} M \text { and [lactate }]=2.9 \mathrm{m} M\) and \(\Delta G\) for the lactate dehydrogenase reaction \(=-15 \mathrm{kJ} / \mathrm{mol}\) in erythrocytes, what is the \(\left[\mathrm{NAD}^{+}\right] /[\mathrm{NADH}]\) ratio under these conditions?

In problem 18 at the end of Chapter \(19,\) you might have calculated the number of molecules of oxaloacetate in a typical mitochondrion. What about protons? A typical mitochondrion can be thought of as a cylinder \(1 \mu \mathrm{m}\) in diameter and \(2 \mu \mathrm{m}\) in length. If the \(\mathrm{pH}\) in the matrix is \(7.8,\) how many protons are contained in the mitochondrial matrix?

a. What is the standard free energy change \(\left(\Delta G^{\circ}\right)\) for the reduction of coenzyme \(\mathrm{Q}\) by \(\mathrm{NADH}\) as carried out by Complex \(\mathrm{I}\) (NADH-coenzyme Q reductase) of the electron-transport pathway if \(\mathscr{E}_{\mathrm{o}}^{\prime}\left(\mathrm{NAD}^{+} / \mathrm{NADH}\right)=-0.320 \mathrm{V}\) and \(\mathscr{E}_{\mathrm{o}}^{\prime}\left(\mathrm{CoQ} / \mathrm{CoQH}_{2}\right)=\) \(+0.060 \mathrm{V}\) b. What is the equilibrium constant \(\left(K_{\mathrm{eq}}\right)\) for this reaction? c. Assume that (1) the actual free energy release accompanying the NADH- coenzyme Q reductase reaction is equal to the amount released under standard conditions (as calculated in part a \(),(2)\) this energy can be converted into the synthesis of ATP with an efficiency \(=0.75\) (that is, \(75 \%\) of the energy released upon NADH oxidation is captured in ATP synthesis), and (3) the oxidation of 1 equivalent of NADH by coenzyme Q leads to the phosphorylation of 1 equivalent of ATP. Under these conditions, what is the maximum ratio of [ATP]/ \([\mathrm{ADP}]\) attainable by oxidative phosphorylation when \(\left[\mathrm{P}_{\mathrm{i}}\right]=1 \mathrm{m} M ?\) (Assume \(\Delta G^{\circ \prime}\) for ATP synthesis \(=+30.5 \mathrm{kJ} / \mathrm{mol}\).)

Consider the oxidation of NADH by molecular oxygen as carried out via the electron-transport pathway \\[ \mathrm{NADH}+\mathrm{H}^{+}+\frac{1}{2} \mathrm{O}_{2} \longrightarrow \mathrm{NAD}^{+}+\mathrm{H}_{2} \mathrm{O} \\] a. What is the standard free energy change \(\left(\Delta G^{\circ}\right)\) for this reaction if \(\mathscr{E}_{\mathrm{o}}^{\prime}\left(\mathrm{NAD}^{+} / \mathrm{NADH}\right)=-0.320 \mathrm{V}\) and \(\mathscr{E}_{\mathrm{o}}^{\prime}\left(\mathrm{O}_{2} / \mathrm{H}_{2} \mathrm{O}\right)=\) \\[ +0.816 \mathrm{V} \\] b. What is the equilibrium constant \(\left(K_{\mathrm{cq}}\right)\) for this reaction? c. Assume that (1) the actual free energy release accompanying NADH oxidation by the electron-transport pathway is equal to the amount released under standard conditions (as calculated in part \(a),(2)\) this energy can be converted into the synthesis of ATP with an efficiency \(=0.75\) (that is, \(75 \%\) of the energy released upon NADH oxidation is captured in ATP synthesis), and (3) the oxidation of 1 NADH leads to the phosphorylation of 3 equivalents of ATP. Under these conditions, what is the maximum ratio of [ATP]/ \([\mathrm{ADP}]\) attainable by oxidative phosphorylation when \(\left[\mathrm{P}_{\mathrm{i}}\right]=2 \mathrm{m} M ?\) (Assume \(\Delta G^{\circ \prime}\) for ATP synthesis \(=+30.5 \mathrm{kJ} / \mathrm{mol}\).)

Considering that all other dehydrogenases of glycolysis and the TCA cycle use NADH as the electron donor, why does succinate dehydrogenase, a component of the TCA cycle and the electron transfer chain, use FAD as the electron acceptor from succinate, rather than \(\mathrm{NAD}^{+}\) ? Note that there are two justifications for the choice of FAD here-one based on energetics and one based on the mechanism of electron transfer for FAD versus \(\mathrm{NAD}^{+}\).
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