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Chapter 15: Problem 35

Cytochrome \(c\) is easily dissociated from isolated mitochondrial membrane preparations, but the isolation of cytochrome \(c_{1}\) requires the use of strong detergents. Explain why.

Short Answer

Expert verified
Cytochrome \(c\) is a loosely associated peripheral protein, easily dissociated, whereas cytochrome \(c_1\) is an integral protein, requiring strong detergents for isolation.

Step by step solution

01

Understanding Cytochrome c Location

Cytochrome \(c\) is a peripheral membrane protein, which means it is loosely attached to the surface of the inner mitochondrial membrane. Because of this loose association, it can be more easily dissociated with mild treatments such as salt solutions or changes in pH.
02

Understanding Cytochrome c1 Location

Cytochrome \(c_1\) is part of the cytochrome \(bc_1\) complex (Complex III) embedded within the inner mitochondrial membrane. It is an integral membrane protein, meaning it is tightly integrated into the lipid bilayer or complex structure of the membrane.
03

Explaining the Association Strength

The strong association of cytochrome \(c_1\) with the membrane is due to its integral nature, requiring detergents to break the membrane apart. Detergents solubilize the lipids in which the protein is embedded, thereby allowing the extraction of \(c_1\).
04

Conclusion

Since cytochrome \(c\) is only loosely attached to the external surface of the inner mitochondrial membrane, it can be easily removed. In contrast, cytochrome \(c_1\) is strongly embedded within the membrane, necessitating harsh treatments for isolation.

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Key Concepts

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

Peripheral Membrane Protein
Peripheral membrane proteins, such as cytochrome \(c\), are intriguing components of cell membranes. These proteins are not anchored deeply within the membrane itself but are more loosely linked to the outer or inner surfaces. They can attach to the membrane through various interactions such as hydrogen bonds, ionic bonds, or through interactions with integral membrane proteins. Since their attachment is more superficial, peripheral membrane proteins are easier to isolate.

When considering the ease of separation, think of the peripheral membrane proteins as guests at a party. They stay close, interact and communicate, but they aren鈥檛 foundational members. Their role is often essential but does not require being embedded into the core structure. This lighter connection allows for their removal through methods like altering pH or ion concentrations.
  • Loosely attached to membrane surfaces
  • Can be dissociated using mild solutions
  • Typically interact with other nearby molecules or proteins
Integral Membrane Protein
Integral membrane proteins, such as cytochrome \(c_1\), represent a crucial component of cell membranes. These proteins are embedded within the lipid bilayer of the membrane and are often involved in precise cellular functions. Their integration means that parts of the protein reside within the hydrophobic core of the membrane, anchoring them firmly.

Unlike peripheral proteins, integral proteins are like the pillars of a building 鈥� they form an essential structural component. Hence, removing them requires more drastic measures. Special agents like detergents break the tight membrane connections, allowing scientists to study these proteins in isolation.
  • Embedded within the lipid bilayer
  • Functions often involve transport or communication across the membrane
  • Extraction requires the use of detergents
Mitochondrial Membrane
The mitochondrial membrane is a key player in cellular energy production. It consists of two layers: the outer membrane and the inner membrane. The inner membrane houses several important complexes, one of which is the cytochrome \(bc_1\) complex that contains cytochrome \(c_1\).

This membrane supports various functions vital for ATP production. Its unique structure allows it to maintain a delicate balance between permeability and protection, enabling mitochondria to function efficiently. The inner membrane is the site for the electron transport chain (ETC), where cytochromes take part in electron transfer.
  • Composed of two distinct lipid bilayers
  • Internal environment crucial for ATP synthesis
  • Hosts the electron transport chain

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Most popular questions from this chapter

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.

In experimental systems, the \(\mathrm{F}_{0}\) component of ATP synthase can be reconstituted into a membrane. \(F_{0}\) can then act as a proton channel that is blocked when the \(\mathrm{F}_{1}\) component is added to the system. What molecule must be added to the system in order to restore the protontranslocating activity of \(\mathrm{F}_{0}\) ? Explain.

Calculate the free energy change for transporting a proton out of the mitochondrial matrix when \(\mathrm{pH}_{\text {matrix }}=7.55, \mathrm{pH}_{\text {cytosal }}=7.35\), \(\Delta \Psi=170 \mathrm{mV}\), and \(T=37^{\circ} \mathrm{C}\).

At one time, it was believed that myoglobin functioned simply as an oxygen- storage protein. New evidence suggests that myoglobin plays a much more active role in the muscle cell. The phrase myoglobinfacilitated oxygen diffusion describes myoglobin's role in transporting oxygen from the muscle cell sarcolemma to the mitochondrial membrane surface. Mice in which the myoglobin gene was knocked out had higher tissue capillary density, elevated red blood cell counts, and increased coronary blood flow. Explain the reasons for these compensatory mechanisms in the knockout mice.

The Eastern skunk cabbage can maintain its temperature \(15-35^{\circ} \mathrm{C}\) higher than ambient temperature during the months of February and March, when ambient temperatures range from \(-15\) to \(+15^{\circ} \mathrm{C}\). Thermogenesis in the skunk cabbage is critical to the survival of the plant since the spadix (a flower component) is not frost-resistant. An uncoupling protein is responsible for the observed thermogenesis. a. The spadix relies on the skunk cabbage's massive root system, which stores appreciable quantities of starch. Why is a large quantity of starch required for the skunk cabbage to carry out sustained thermogenesis for weeks rather than hours? b. Oxygen consumption by the skunk cabbage increases as the temperature decreases, nearly doubling with every \(10^{\circ} \mathrm{C}\) drop in ambient temperature. Oxygen consumption was observed to decrease during the day, when temperatures were close to \(30^{\circ} \mathrm{C}\), and increase at night. What is the biochemical explanation for these observations?
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