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Why is succinate oxidized by FAD instead of by \(\mathrm{NAD}^{+}\)?

Short Answer

Expert verified
Succinate is oxidized by FAD, not by \( \mathrm{NAD}^+ \), because FAD has a higher redox potential.

Step by step solution

01

Understand the Redox Potentials

The choice of electron carriers is determined by their redox potential, which is a measure of the tendency of a chemical species to acquire electrons and thereby be reduced. \( \mathrm{NAD}^+ \) has a redox potential of approximately \(-0.32\, \mathrm{V} \), while FAD has a redox potential of approximately \(-0.22\, \mathrm{V} \). This means that FAD is more capable of accepting electrons from succinate than \( \mathrm{NAD}^+ \).
02

Identify the Electron Donor

Succinate, the substrate in the cycle, has a relatively low ability to donate electrons, which means it requires an electron acceptor with a slightly higher redox potential than \( \mathrm{NAD}^+ \) can provide. Since FAD has a higher redox potential than \( \mathrm{NAD}^+ \), it is more suitable for oxidizing succinate.
03

Compare Energetic Favorability

Electron transfers are only energetically favorable if they go from lower to higher redox potential. In the case of succinate oxidation, the electron transfer to FAD is favorable due to its higher redox potential. If \( \mathrm{NAD}^+ \) was used, the reaction would not proceed efficiently since the redox potential difference would not favor electron transfer.

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Key Concepts

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

Electron Carriers
In biochemical reactions, electron carriers play a crucial role. These molecules, like FAD and \( \mathrm{NAD}^+ \), help in transferring electrons during oxidation-reduction (redox) reactions. This transfer is fundamental for cellular processes, such as respiration and energy production. Electron carriers have specific redox potentials that express their ability to accept or donate electrons.
  • FAD (Flavin Adenine Dinucleotide) can accept two electrons, becoming FADH2.
  • \( \mathrm{NAD}^+ \) (Nicotinamide Adenine Dinucleotide) accepts electrons and becomes \( \mathrm{NADH} \).
The choice between FAD and \( \mathrm{NAD}^+ \) depends on their capacities to accommodate electrons from specific substrates. This is why FAD is preferred for succinate oxidation, as it can better stabilize the carried electrons due to its higher redox potential.
Redox Potential
Redox potential, or reduction potential, is a crucial determinant in redox reactions. It measures a molecule's ability to attract electrons. The potential is expressed in volts, indicating the tendency of a substance to gain electrons and be reduced. The higher the redox potential, the stronger the affinity for electrons.
  • \( \mathrm{NAD}^+ \) has a lower redox potential (\(-0.32 \mathrm{V}\)), making it less suitable for certain reactions.
  • FAD, with a redox potential of \(-0.22 \mathrm{V}\), indicates a greater readiness to accept electrons compared to \( \mathrm{NAD}^+ \).
In the oxidation of succinate, FAD's higher redox potential is essential. It allows the reaction to proceed efficiently, as electrons are more naturally transferred from succinate to FAD than to \( \mathrm{NAD}^+ \). This ensures the energetic favorability and continuation of metabolic processes.
Biochemical Oxidation
Biochemical oxidation is a critical process in living cells, where substrates like succinate lose electrons, effectively giving them up to electron carriers. This loss of electrons is essential for energy generation in biochemical pathways, such as the Krebs cycle. In these processes, the choice of electron carrier affects the pathway's efficiency.
  • The oxidation of succinate involves its electrons being transferred to FAD.
  • This step is part of the larger process of energy extraction from fuels that organisms consume.
By understanding biochemical oxidation, one grasps the movement of electrons in cellular respiration. The choice of electron carrier significantly impacts how well these electrons are transferred, which in turn influences how effectively a cell can produce energy from different substrates. The selection of FAD over \( \mathrm{NAD}^+ \) for succinate is a direct result of these chemical preferences and potentials.

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Most popular questions from this chapter

Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease that causes muscle paralysis and eventually death. Researchers measured the activity of the electron transport chain complexes in various regions of the nervous system in patients with ALS. In a certain region of the spinal cord, Complex I showed decreased activity but not decreased concentration. How does this contribute to progression of the disease?

Complex I, succinate dehydrogenase, acyl-CoA dehydrogenase, and glycerol-3-phosphate dehydrogenase (see Fig. 15.11) are all flavoproteins; that is, they contain an FMN or FAD prosthetic group. Explain the function of the flavin group in these enzymes. Why are the flavoproteins ideally suited to transfer electrons to ubiquinone?

Chromium is most toxic and highly soluble in its oxidized \(\mathrm{Cr}(\mathrm{VI})\) state but is less toxic and less soluble in its more reduced \(\mathrm{Cr}\) (III) state. Efforts to detoxify Cr-contaminated groundwater have involved injecting chemical reducing agents underground. Another approach is bioremediation, which involves injecting molasses or cooking oil into the contaminated groundwater. Explain how these substances would promote the reduction of \(\mathrm{Cr}\) (VI) to \(\mathrm{Cr}\) (III).

UCP1 is an uncoupling protein in brown fat (Box 15.B). Experiments using UCP1-knockout mice (animals missing the gene for UCP1) resulted in the discovery of a second uncoupling protein named UCP2. a. Oxygen consumption increased over twofold when a \(\beta_{3}\) adrenergic agonist that stimulates UCP1 was injected into normal mice. This was not observed when the agonist was injected into the knockout mice. Explain these results. b. In one experiment, normal mice and UCP1-knockout mice were placed in a cold \(\left(5^{\circ} \mathrm{C}\right)\) room overnight. The normal mice were able to maintain their body temperature at \(37^{\circ} \mathrm{C}\) even after 24 hours in the cold. But the body temperatures of the cold-exposed knockout mice decreased \(10^{\circ} \mathrm{C}\) or more. Explain.

Ubiquinone is not anchored in the mitochondrial membrane but is free to diffuse laterally throughout the membrane among the electron transport chain components. What aspects of its structure account for this behavior?

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