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All Parts of Ubiquinone Have a Function In electron transfer, only the quinone portion of ubiquinone undergoes oxidation-reduction; the isoprenoid side chain remains unchanged. What is the function of this chain?

Short Answer

Expert verified
The isoprenoid side chain anchors ubiquinone in the mitochondrial membrane, aiding electron transfer.

Step by step solution

01

Identify Ubiquinone's Structure

Ubiquinone, often called coenzyme Q, is a molecule with a distinct structure. It has a quinone ring and a long isoprenoid side chain. Understanding this structure is critical for determining the function of each part of the molecule.
02

Recognize Function of the Quinone Ring

The quinone ring in ubiquinone undergoes oxidation and reduction. It plays a crucial role in electron transfer in the electron transport chain (ETC), where it accepts and donates electrons. This is critical for the production of ATP in cellular respiration.
03

Investigate Function of the Isoprenoid Side Chain

While the quinone head is involved in electron transfer, the isoprenoid side chain does not directly participate in redox reactions. Instead, its primary function is to anchor ubiquinone into the lipid bilayer of the mitochondrial inner membrane due to its hydrophobic properties. This localization is essential for ubiquinone to effectively engage in electron transfer within the ETC.
04

Conclusion on Isoprenoid Side Chain Function

The isoprenoid side chain's role is not to participate directly in electron transfer but to ensure that ubiquinone is situated correctly within the mitochondrial inner membrane, allowing the quinone head to perform its function effectively in the electron transport process.

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Key Concepts

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

Electron Transport Chain
The electron transport chain (ETC) is a critical component of cellular respiration, which takes place in the mitochondria of cells. It is a series of protein complexes and molecules that transfer electrons through redox (reduction-oxidation) reactions. This transfer is essential for the formation of an electrochemical gradient that drives the synthesis of ATP, the main energy currency of the cell.
  • In the ETC, electrons are passed along a chain of proteins and other molecules, including ubiquinone, which plays a vital role in shuttling electrons between complexes.
  • This process begins with electrons donated by NADH and FADH2, which are produced during earlier stages of cellular respiration.
  • As electrons move through the chain, they release energy that actively pumps protons across the mitochondrial membrane, creating a proton gradient.
  • The final electron acceptor in the chain is oxygen, which combines with protons to form water, a byproduct of respiration.
Understanding the ETC is crucial as it is the primary pathway through which cells harness energy from nutrients.
Oxidation-Reduction
Oxidation-reduction, often abbreviated as redox, refers to chemical reactions in which the oxidation state of atoms is changed. These reactions involve the transfer of electrons between molecules. In the context of the electron transport chain, redox reactions are fundamental to the functioning of this system.
  • Oxidation involves the loss of electrons, while reduction involves the gain of electrons.
  • Ubiquinone, a key player in the ETC, undergoes redox reactions as it accepts and donates electrons between complex I and complex III.
  • The ability of ubiquinone to toggle between oxidized and reduced states makes it a crucial mediator in these electron transfers.
  • As electrons are transferred, the energy released is used to pump protons across the membrane, which is essential for ATP synthesis.
Redox reactions ensure a continuous flow of electrons, facilitating ongoing energy production within cells.
Isoprenoid Side Chain
The isoprenoid side chain of ubiquinone does not participate directly in electron transfer. Instead, it has a structural and supportive role within the electron transport chain.
  • This long hydrocarbon chain imparts hydrophobic properties to ubiquinone, allowing it to embed itself firmly within the lipid bilayer of the mitochondrial inner membrane.
  • By anchoring ubiquinone, the isoprenoid side chain ensures that the molecule remains properly oriented and localized to function effectively in the ETC.
  • This proper localization is critical for the quinone ring to access and transfer electrons efficiently.
  • The integration of ubiquinone within the membrane structure underscores the importance of its side chain in maintaining cellular organization and function.
Thus, the isoprenoid side chain plays an indirect yet vital role in mitochondrial energy metabolism.
Mitochondrial Inner Membrane
The mitochondrial inner membrane is a highly specialized and integral component of the mitochondrion, the powerhouse of the cell. It serves several critical roles directly related to cellular energy production.
  • This membrane is the site where the electron transport chain (ETC) is located, enabling it to function as the central hub of ATP production.
  • It is richly embedded with proteins, including the complexes of the ETC, ensuring efficient electron flow and ATP synthesis.
  • The inner membrane's impermeability to protons is key to establishing the proton gradient required for ATP production.
  • Furthermore, molecules like ubiquinone reside in this membrane, where their unique properties support the ETC's operation.
  • This environment facilitates the conversion of potential energy from the proton gradient into chemical energy stored in ATP.
The structure and composition of the mitochondrial inner membrane are pivotal for efficient energy conversion, making it essential for life-sustaining processes.

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Most popular questions from this chapter

Transmembrane Movement of Reducing Equivalents Under aerobic conditions, extramitochondrial NADH must undergo oxidation by the mitochondrial respiratory chain. Consider a preparation of rat hepatocytes containing mitochondria and all the cytosolic enzymes. After the introduction of \(\left[4-{ }^{3} \mathrm{H}\right] \mathrm{NADH}\), radioactivity soon appears in the mitochondrial matrix. Conversely, no radioactivity appears in the matrix after the introduction of \(\left[7^{-14} \mathrm{C}\right]\) NADH. What do these observations reveal about the oxidation of extramitochondrial NADH by the respiratory chain?

Use of FAD Rather Than NAD \(^{+}\)in Succinate Oxidation All the dehydrogenases of glycolysis and the citric acid cycle use \(\mathrm{NAD}^{+}\left(E^{\prime \circ}\right.\) for \(\mathrm{NAD}^{+} / \mathrm{NADH}\) is \(\left.-0.32 \mathrm{~V}\right)\) as electron acceptor except succinate dehydrogenase, which uses covalently bound \(\mathrm{FAD}\left(E^{\prime \circ}\right.\) for \(\mathrm{FAD}^{+} / \mathrm{FADH}_{2}\) in this enzyme is \(0.050 \mathrm{~V}\) ). Suggest why FAD is a more appropriate electron acceptor than \(\mathrm{NAD}^{+}\)in the dehydrogenation of succinate, based on the \(E^{\prime \circ}\) values of fumarate/succinate \(\left(E^{\prime \circ}=0.031 \mathrm{~V}\right), \mathrm{NAD}^{+} / \mathrm{NADH}\), and the succinate dehydrogenase \(\mathrm{FAD} / \mathrm{FADH}_{2}\).

Mitochondrial Disease and Cancer Mutations in the genes that encode certain mitochondrial proteins are associated with a high incidence of some types of cancer. How might defective mitochondria lead to cancer?

Time Scales of Regulatory Events in Mitochondria Compare the likely time scales for the adjustments in respiratory rate caused by a. increased [ADP] and b. reduced \(\mathrm{pO}_{2}\). What accounts for the difference?

Reactive Oxygen Species Describe the role played by superoxide dismutase in ameliorating the effects of reactive oxygen species.

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