Mastering Biology Chapter 8

The potential energy of the products is less than the potential energy of the reactants. (If a reaction is exergonic, the formation of new bonds releases more energy than was invested in breaking the old bonds.)

Energy input into the organism must be occurring to drive the decrease in entropy. (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.)

- An increase in concentration of enzyme - Increasing the substrate concentration (Either increasing the enzyme concentration or slightly increasing the temperature will increase the rate of product formation)

The negatively charged phosphate groups vigorously repel one another and the terminal phosphate group is more stable in water than it is in ATP. (Negative charges repel each other. Loss of the terminal phosphate removes some of the repulsion)

By locally concentrating the reactants (One of the ways enzymes work is to increase the concentrations of reactants at a single place.)

The aerobic respiration of one molecule of glucose produces six molecules each of carbon dioxide and water. (The second law of thermodynamics states that every energy transformation makes the universe more disordered--carbon dioxide and water are more disordered than glucose)

The hydrolysis of ATP (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 molecules, such as glucose)

In the cell, the hydrolysis of ATP is coupled to other endergonic reactions. (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.)

The active site may resemble a groove or pocket in the surface of a protein into which the substrate fits. (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.)

Neither the sign nor the magnitude of Delta G has anything to do with the speed of a reaction. (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)

Allosteric activation (This molecule in this example would be termed an allosteric activator)

The enzyme changes its shape slightly as the substrate binds to it. (the enzyme changes slightly to bind to the substrate and catalyze the reaction)

Organisms acquire energy from, and lose energy to, their surroundings. (Open systems are those in which energy and materials can be exchanged between the system and its surroundings)

Delta G is negative. (In an endergonic reaction, in which order is increased, the change in entropy, symbolized by DeltaS, is negative.)

There is too little activation energy available...(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.)

The reaction that proceeds to convert A and B to C and D is endergonic; the products are more organized that the reactants. (C and D contain more energy than do A and B; therefore they are more organized and their construction required an input of energy.)

None of the answers are correct. (Changes in temp. substrate concentration, and pH are all likely to affect enzyme activity)

The activation energy. (An enzyme lowers the amount of energy required to get the reactants to the transition state.)

glucose + fructose --> sucrose (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.)

Delta G (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.)

To obey the first law, the crops must represent an open system. (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.)

high or low pH may disrupt hydrogen bonding or ionic interactions and thus change the shape of the active site. (Each enzyme has an optimal pH at which it is most active, and variations in pH can alter the enzyme's structure, changing activity)

- The continuous removal of the products of a pathway to be used in other reactions. - An input of heat from the environment. (Pathways can be displaced from equilibrium either by adding free energy or by removal of the products of the pathway by other reactions.)

The free energy released by ATP hydrolysis may be coupled to an endergonic process via the formation of a phosphorylated intermediate. (This is one way a cell can use an exergonic reaction to drive an endergonic reaction.)

A decrease in the system's total energy will increase the probability of spontaneous change, increasing the entropy of a system will increase the probability of spontaneous change, and increasing the temperature of a system will increase the probability of spontaneous change.

Anabolic pathways synthesize more complex organic molecules using the energy derived from catabolic pathways. (The synthesis of complex molecules in anabolic pathways requires an input of energy from catabolic pathways.)

Releases energy when proceeding in the forward direction. (exergonic reactions proceed with a net release of free energy, and they occur spontaneously.)

Enzymes can lower the activation energy of reactions, but they cannot change the equilibrium point because they cannot change the net energy output. (Enzymes lower the activation energy barrier of a reaction but do not change the free energy of the products.)

Succinylcholine must be a competitive inhibitor with acetylcholine. (Competitive inhibition occurs when a molecule mimics the substrate by competing with it at the active site.)

The free energy of the reactants and the free energy of the products. (By subtracting the free energy of the reactants form the free energy of the products, the DeltaG can be calculated and the difference in these values determines the sign of the difference.)

- They are sensitive to environmental conditions - They exist in active and inactive conformations - They are acted on by inhibitors.

- Heat from the environment is necessary for substrates to get over the activation energy barrier - Increasing the amount of heat in a system will always increase the rate of enzyme-catalyzed reactions. (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.)

Proton movement against a gradient of protons. (Protein pumps that hydrolyze ATP can generate electrochemical gradients)

An enzyme is consumed during the reaction it catalyzes. (if enzymes were consumed during the reaction they catalyzed, they would not be able to act as a catalyst.)

A starch molecule. (Starch is a large polymer of sugar and thus contains many covalent bonds.)