Which of the following correctly states the relationship between anabolic and catabolic pathways? (see book section: Concept 8.1: An organism’s metabolism transforms matter and energy, subject to the laws of thermodynamics) A) Catabolic pathways produce usable cellular energy by synthesizing more complex organic molecules. |
Anabolic pathways synthesize more complex organic molecules using the energy derived from catabolic pathways. Correct. The synthesis of complex molecules in anabolic pathways requires an input of energy from catabolic pathways. |
Which of the following situations does not represent an energy transformation? (see book section: Concept 8.1: An organism’s metabolism transforms matter and energy, subject to the laws of thermodynamics) A) the production of sugars from carbon dioxide and water during photosynthesis |
the coupling of ATP hydrolysis to the production of a proton gradient across a membrane by a proton pump Correct. The energy stored in ATP is used to create an electrochemical gradient of protons that contains energy. |
Organisms are described as thermodynamically open systems. Which of the following statements is consistent with this description? (see book section: Concept 8.1: An organism’s metabolism transforms matter and energy, subject to the laws of thermodynamics) A) Because energy must be conserved, organisms constantly recycle energy and thus need no input of energy. |
Organisms acquire energy from, and lose energy to, their surroundings. Correct. Open systems are those in which energy and materials can be exchanged between the system and its surroundings. |
Consider the growth of a farmer’s crop over a season. Which of the following correctly states a limitation imposed by the first or second law of thermodynamics? (see book section: Concept 8.1: An organism’s metabolism transforms matter and energy, subject to the laws of thermodynamics) A) To obey the first law, the crops must represent an open system. |
To obey the first law, the crops must represent an open system. Correct. The first law states that energy cannot be created. The growth of plants stores much energy in the body of the plant. That energy must have been obtained from the plant’s environment; thus, the plant must be an open system. |
Which of the following states the relevance of the first law of thermodynamics to biology? (see book section: Concept 8.1: An organism’s metabolism transforms matter and energy, subject to the laws of thermodynamics) A) Energy is destroyed as glucose is broken down during cellular respiration |
Energy can be freely transformed among different forms as long as the total energy is conserved. Correct. The first law of thermodynamics states that energy can be transformed but can be neither created nor destroyed. |
Which is the most abundant form of energy in a cell? (see book section: Concept 8.1: An organism’s metabolism transforms matter and energy, subject to the laws of thermodynamics) A) kinetic energy |
chemical energy Correct. All of the macromolecules that make up a cell contain large amounts of chemical (potential) energy, stored when they were made in anabolic reactions |
Which of the following is an example of the second law of thermodynamics as it applies to biological reactions? (see book section: Concept 8.1: An organism’s metabolism transforms matter and energy, subject to the laws of thermodynamics) A) The aerobic respiration of one molecule of glucose produces six molecules each of carbon dioxide and water. |
The aerobic respiration of one molecule of glucose produces six molecules each of carbon dioxide and water. Correct. The second law of thermodynamics states that every energy transformation makes the universe more disordered—carbon dioxide and water are more disordered than glucose. |
According to the second law of thermodynamics, which of the following is true? (see book section: Concept 8.1: An organism’s metabolism transforms matter and energy, subject to the laws of thermodynamics) A) The entropy of the universe is constantly decreasing. |
The decrease in entropy associated with life must be compensated for by increased entropy in the environment in which life exists. Correct. The second law of thermodynamics demands that total entropy must increase with any reaction. |
If the entropy of a living organism is decreasing, which of the following is most likely to be occurring simultaneously? (see book section: Concept 8.2: The free-energy change of a reaction tells us whether or not the reaction occurs spontaneously) A) In this situation, the second law of thermodynamics must not apply. |
Energy input into the organism must be occurring to drive the decrease in entropy. Correct. If the entropy is decreasing, this would tend to make the free energy change associated with this positive. Thus, an input of energy would be required to make this decrease in entropy occur. |
Which of the following has the most free energy per molecule? (see book section: Concept 8.2: The free-energy change of a reaction tells us whether or not the reaction occurs spontaneously) A) a sugar molecule |
a starch molecule Correct. Starch is a large polymer of sugar and thus contains many covalent bonds. |
The electronic arrangement in which of the following molecules means that this (these) molecule(s) has/have greater free energy than the others? (see book section: Concept 8.2: The free-energy change of a reaction tells us whether or not the reaction occurs spontaneously) A) methane |
methane Correct. Bonds that contain electrons that are more equally shared between atoms release more energy when the electrons from those bonds are used to form lower energy bonds. |
Which part of the equation ΔG = ΔH – TΔS tells you if a process is spontaneous? (see book section: Concept 8.2: The free-energy change of a reaction tells us whether or not the reaction occurs spontaneously) A) ΔG |
ΔG Correct. In any spontaneous process, the free energy of a system decreases. The change in free energy equals the change in total energy minus the change in entropy times the temperature. |
If, during a process, the system becomes more ordered, then _____. (see book section: Concept 8.2: The free-energy change of a reaction tells us whether or not the reaction occurs spontaneously) A) ΔG is positive |
ΔS is negative Correct. In an endergonic reaction, in which order is increased, the change in entropy, symbolized by ΔS, is negative. |
When one molecule is broken down into six component molecules, which of the following will always be true? (see book section: Concept 8.2: The free-energy change of a reaction tells us whether or not the reaction occurs spontaneously) A) ΔS is negative. |
ΔS is positive. Correct. The large increase in disorder associated with this reaction means that entropy (ΔS) increases |
From the equation ΔG = ΔH – TΔS it is clear that _____. (see book section: Concept 8.2: The free-energy change of a reaction tells us whether or not the reaction occurs spontaneously) A) a decrease in the system’s total energy will increase the probability of spontaneous change |
The first three choices are correct. |
An exergonic (spontaneous) reaction is a chemical reaction that _____. (see book section: Concept 8.2: The free-energy change of a reaction tells us whether or not the reaction occurs spontaneously) A) occurs only when an enzyme or other catalyst is present |
releases energy when proceeding in the forward direction Correct. Exergonic reactions proceed with a net release of free energy, and they occur spontaneously. |
Which of the following reactions would be endergonic? (see book section: Concept 8.2: The free-energy change of a reaction tells us whether or not the reaction occurs spontaneously) A) C6H12O6 + 6 O2 → 6 CO2 + 6 H2O |
glucose + fructose → sucrose Correct. In this case, the product is more complex (lower entropy) than the reactants, and like many anabolic reactions, this one requires an input of energy. |
Molecules A and B contain 110 kcal/mol of free energy and molecules B and C contain 150 kcal/mol of energy. A and B are converted to C and D. What can be concluded? (see book section: Concept 8.2: The free-energy change of a reaction tells us whether or not the reaction occurs spontaneously) A) A and B will be converted to C and D with a net release of energy. |
The reaction that proceeds to convert A and B to C and D is endergonic; the products are more organized than the reactants. Correct. C and D contain more energy than do A and B; therefore they are more organized and their construction required an input of energy |
Which of the following determines the sign of ΔG for a reaction? (see book section: Concept 8.2: The free-energy change of a reaction tells us whether or not the reaction occurs spontaneously) A) the free energy of the products |
the free energy of the reactants and the free energy of the products Correct. By subtracting the free energy of the reactants from the free energy of the products, the ΔG can be calculated and the difference in these values determines the sign of the difference. |
Metabolic pathways in cells are typically far from equilibrium. Which of the following processes tend(s) to keep these pathways away from equilibrium? (see book section: Concept 8.2: The free-energy change of a reaction tells us whether or not the reaction occurs spontaneously) A) the continuous removal of the products of a pathway to be used in other reactions |
The first and second listed responses are correct. Correct. Pathways can be displaced from equilibrium either by adding free energy or by removal of the products of the pathway by other reactions. |
Which of the following is an example of the cellular work accomplished with the free energy derived from the hydrolysis of ATP, involved in the production of electrochemical gradients? (see book section: Concept 8.3: ATP powers cellular work by coupling exergonic reactions to endergonic reactions) A) proton movement against a gradient of protons |
proton movement against a gradient of protons Correct. Protein pumps that hydrolyze ATP can generate electrochemical gradients. |
In general, the hydrolysis of ATP drives cellular work by _____. (see book section: Concept 8.3: ATP powers cellular work by coupling exergonic reactions to endergonic reactions) A) acting as a catalyst |
releasing free energy that can be coupled to other reactions Correct. With the help of specific enzymes, the cell can couple the energy of ATP hydrolysis directly to endergonic processes. |
Which of the following statements correctly describes some aspect of ATP hydrolysis being used to drive the active transport of an ion into the cell against the ion’s concentration gradient? (see book section: Concept 8.2: The free-energy change of a reaction tells us whether or not the reaction occurs spontaneously and see book section: Concept 8.3: ATP powers cellular work by coupling exergonic reactions to endergonic reactions) A) The hydrolysis of ATP is endergonic, and the active transport is exergonic. |
This is an example of energy coupling. Correct. The free energy released from the hydrolysis of ATP is coupled to the energy-requiring active transport of the ion across a membrane. |
Much of the suitability of ATP as an energy intermediary is related to the instability of the bonds between the phosphate groups. These bonds are unstable because _____. (see book section: Concept 8.3: ATP powers cellular work by coupling exergonic reactions to endergonic reactions) A) the valence electrons in the phosphorus atom have less energy on average than those of other atoms |
the negatively charged phosphate groups vigorously repel one another and the terminal phosphate group is more stable in water than it is in ATP |
When 1 mole of ATP is hydrolyzed in a test tube without an enzyme, about twice as much heat is given off as when 1 mole of ATP is hydrolyzed in a cell. Which of the following best explains these observations? (see book section: Concept 8.3: ATP powers cellular work by coupling exergonic reactions to endergonic reactions) A) In cells, ATP is hydrolyzed to ADP and Pi, but in the test tube it is hydrolyzed to carbon dioxide and water. |
In the cell, the hydrolysis of ATP is coupled to other endergonic reactions. Correct. The coupling of ATP to other endergonic processes in cells means that less of the free energy is released as heat. When ATP is hydrolyzed without this coupling, all of the energy is released as heat. |
What best characterizes the role of ATP in cellular metabolism? (see book section: Concept 8.3: ATP powers cellular work by coupling exergonic reactions to endergonic reactions) A) The DG associated with its hydrolysis is positive. |
The free energy released by ATP hydrolysis may be coupled to an endergonic process via the formation of a phosphorylated intermediate. |
The formation of glucose-6-phosphate from glucose is an endergonic reaction and is coupled to which of the following reactions or pathways? (see book section: Concept 8.3: ATP powers cellular work by coupling exergonic reactions to endergonic reactions) A) the hydrolysis of ATP |
the hydrolysis of ATP Correct. With the help of specific enzymes, the cell is able to couple the energy of ATP hydrolysis directly to endergonic processes by transferring a phosphate group from ATP to some other molecule, such as glucose. |
A chemical reaction is designated as exergonic rather than endergonic when _____. (see book section: Concept 8.2: The free-energy change of a reaction tells us whether or not the reaction occurs spontaneously and see book section: Concept 8.4: Enzymes speed up metabolic reactions by lowering energy barriers) A) the products are less complex than the reactants |
the potential energy of the products is less than the potential energy of the reactan Correct. If a reaction is exergonic, the formation of new bonds releases more energy than was invested in breaking the old bonds. |
Which of the following is changed by the presence of an enzyme in a reaction? (see book section: Concept 8.2: The free-energy change of a reaction tells us whether or not the reaction occurs spontaneously and see book section: Concept 8.4: Enzymes speed up metabolic reactions by lowering energy barriers) A) the activation energy |
the activation energy Correct. An enzyme lowers the amount of energy required to get the reactants to the transition state. |
What do the sign and magnitude of the ΔG of a reaction tell us about the speed of the reaction? (see book section: Concept 8.2: The free-energy change of a reaction tells us whether or not the reaction occurs spontaneously and see book section: Concept 8.4: Enzymes speed up metabolic reactions by lowering energy barriers) A) The more negative the ΔG, the faster the reaction is. |
Neither the sign nor the magnitude of ΔG have anything to do with the speed of a reaction. Correct. The speed of a reaction is determined by the activation energy barrier of the reaction and the temperature (which determines how many reactants have the energy to overcome the barrier). |
How do enzymes lower activation energy? (see book section: Concept 8.4: Enzymes speed up metabolic reactions by lowering energy barriers) A) by locally concentrating the reactants |
by locally concentrating the reactants Correct. One of the ways enzymes work is to increase the concentrations of reactants at a single place. |
Which of the following statements about enzymes is true? (see book section: Concept 8.4: Enzymes speed up metabolic reactions by lowering energy barriers) A) Enzymes speed up the rate of the reaction without changing the (change in)G for the reaction. |
Enzymes speed up the rate of the reaction without changing the (change in)G for the reaction. Correct. Enzymes speed up reactions by lowering the activation energy barrier for the reaction. Enzymes cannot change the DG for the reaction. |
Which of the following statements about enzyme function is correct? (see book section: Concept 8.4: Enzymes speed up metabolic reactions by lowering energy barriers) A) Enzymes can change the equilibrium point of reactions, but they cannot speed up reactions because they cannot change the net energy output. |
Enzymes can lower the activation energy of reactions, but they cannot change the equilibrium point because they cannot change the net energy output. Correct. Enzymes lower the activation energy barrier of a reaction but do not change the free energy of the products. |
A plot of reaction rate (velocity) against temperature for an enzyme indicates little activity at 10°C and 45°C, with peak activity at 35°C. The most reasonable explanation for the low velocity at 10°C is that _____. (see book section: Concept 8.4: Enzymes speed up metabolic reactions by lowering energy barriers) A) the enzyme was denatured |
there is too little activation energy available Correct. The environment usually supplies activation energy in the form of heat. The lower the temperature, the less energy that is available to overcome the activation energy barrier. |
Which of the following statements about enzymes is incorrect? (see book section: Concept 8.4: Enzymes speed up metabolic reactions by lowering energy barriers) A) Enzymes can be used to accelerate both anabolic and catabolic reactions. |
An enzyme is consumed during the reaction it catalyzes. Correct. If enzymes were consumed during the reaction they catalyzed, they would not be able to act as a catalyst. This statement is incorrect. |
Which of the following statements about the active site of an enzyme is correct? (see book section: Concept 8.4: Enzymes speed up metabolic reactions by lowering energy barriers) A) The structure of the active site is not affected by changes in temperature. |
The active site may resemble a groove or pocket in the surface of a protein into which the substrate fits. Correct. Only a restricted region of an enzyme molecule (the active site) binds to the substrate. Usually, the active site is formed by only a few of the amino acids, with the rest of the protein molecule providing a framework that reinforces the configuration of the active site. |
What is meant by the "induced fit" of an enzyme? (see book section: Concept 8.4: Enzymes speed up metabolic reactions by lowering energy barriers) A) The enzyme structure is altered so that it can be induced to fit many different types of substrate. |
The enzyme changes its shape slightly as the substrate binds to it. Correct. The enzyme changes slightly to bind to the substrate and catalyze the reaction. |
Which of the following statements correctly describe(s) the role(s) of heat in biological reactions? (see book section: Concept 8.4: Enzymes speed up metabolic reactions by lowering energy barriers) A) Heat from the environment is necessary for substrates to get over the activation energy barrier. |
The first and second choices are correct. Correct. As the heat energy in a system increases, so does the kinetic energy of the reactants. As the kinetic energy of the reactants increases, the reactants are more likely to interact (with each other directly, or with the active site of an enzyme). Subsequently, the reaction rate would increase. |
Above a certain substrate concentration, the rate of an enzyme-catalyzed reaction drops as the enzymes become saturated. Which of the following would lead to a faster conversion of substrate into product under these saturated conditions? (see book section: Concept 8.4: Enzymes speed up metabolic reactions by lowering energy barriers) A) an increase in concentration of enzyme |
The first and second listed responses are correct. Correct. Either increasing the enzyme concentration or slightly increasing the temperature will increase the rate of product formation. |
Which of the following environments or actions would not affect the rate of an enzyme reaction? (see book section: Concept 8.4: Enzymes speed up metabolic reactions by lowering energy barriers) A) cooling the enzyme |
None of the listed responses is correct. Correct. Changes in temperature, substrate concentration, and pH are all likely to affect enzyme activity. |
Enzyme activity is affected by pH because _____. (see book section: Concept 8.4: Enzymes speed up metabolic reactions by lowering energy barriers) A) high or low pH may disrupt hydrogen bonding or ionic interactions and thus change the shape of the active site |
high or low pH may disrupt hydrogen bonding or ionic interactions and thus change the shape of the active site Correct. Each enzyme has an optimal pH at which it is most active, and variations in pH can alter the enzyme’s structure, changing activity. |
Which of these statements about enzyme inhibitors is true? (see book section: Concept 8.4: Enzymes speed up metabolic reactions by lowering energy barriers) A) When the product of an enzyme or an enzyme sequence acts as its inhibitor, this is known as positive feedback. |
The action of competitive inhibitors may be reversible or irreversible. Correct. Competitive inhibitors that bind covalently to the enzyme would be irreversible, and those that bind weakly would be reversible. |
Succinylcholine is structurally almost identical to acetylcholine. If succinylcholine is added to a mixture that contains acetylcholine and the enzyme that hydrolyzes acetylcholine (but not succinylcholine), the rate of acetylcholine hydrolysis is decreased. Subsequent addition of more acetylcholine restores the original rate of acetylcholine hydrolysis. Which of the following correctly explains this observation? (see book section: Concept 8.4: Enzymes speed up metabolic reactions by lowering energy barriers) A) Succinylcholine must be a noncompetitive inhibitor. |
Succinylcholine must be a competitive inhibitor with acetylcholine. Correct. Competitive inhibition occurs when a molecule mimics the substrate by competing with it at the active site. |
The process of stabilizing the structure of an enzyme in its active form by the binding of a molecule is an example of _____. (see book section: Concept 8.5: Regulation of enzyme activity helps control metabolism) A) allosteric regulation |
allosteric regulation Correct. The molecule in this example would be termed an allosteric activator. |
Which of the following statements about allosteric proteins is/are true? (see book section: Concept 8.5: Regulation of enzyme activity helps control metabolism) A) They exist in active and inactive conformations. |
All of the first three listed responses are correct. |
The binding of an allosteric inhibitor to an enzyme causes the rate of product formation by the enzyme to decrease. Which of the following best explains why this decrease occurs? (see book section: Concept 8.5: Regulation of enzyme activity helps control metabolism) A) The allosteric inhibitor causes free energy change of the reaction to increase. |
The allosteric inhibitor causes a structural change in the enzyme that prevents the substrate from binding at the active site. Correct. In general, any allosteric regulator functions by changing the structure of the enzyme to either change the ability of the active site to bind the substrate or to facilitate the chemical reaction. |
Under most conditions, the supply of energy by catabolic pathways is regulated by the demand for energy by anabolic pathways. Considering the role of ATP formation and hydrolysis in energy coupling of anabolic and catabolic pathways, which of the following statements is most likely to be true? (see book section: Concept 8.5: Regulation of enzyme activity helps control metabolism) A) High levels of ADP act as an allosteric activator of catabolic pathways |
High levels of ADP act as an allosteric activator of catabolic pathways Correct. In this case, high demand for energy by anabolic pathways uses ATP, increasing the level of ADP, which in turn increases the supply of ATP from catabolic pathways. |
Biology Chapter 8 – CC – Practice Test
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