Degradation of organic molecules by anabolic pathways provides the energy to drive catabolic pathways.
	Energy derived from catabolic pathways is used to drive the breakdown of organic molecules in anabolic pathways.
	Anabolic pathways synthesize more complex organic molecules using the energy derived from catabolic pathways.
	Catabolic pathways produce usable cellular energy by synthesizing more complex organic molecules.
	The flow of energy between catabolic and anabolic pathways is reversible.

	the burning of gasoline in a car engine to move a car
	the production of sugar by photosynthesis
	the production of electrical power by damming a river
	a collision between one billiard ball and other balls, causing them to move
	playing music by putting new batteries in your CD player

	The metabolism of an organism is isolated from its surroundings.
	Cells can freely exchange energy and materials with their environment.
	Organisms acquire energy from their surroundings.
	Heat produced by the organism is conserved in the organism and not lost to the environment.
	Because energy must be conserved, organisms constantly recycle energy and thus need no input of energy.

	The entropy of the universe must decrease in order to account for the increased entropy associated with plant growth.
	The process of photosynthesis produces energy that the plant uses to grow.
	In order to obey the first law, the crop must represent an open system.
	Growth of the crops must occur spontaneously.
	All of the above are correct.

	The total energy taken in by an organism must be greater than the total energy stored or released by the organism.
	Energy can be freely transformed among different forms as long as the total energy is conserved.
	Photosynthetic organisms produce energy in sugars from sunlight.
	All organisms must produce some heat as a result of the processes of life.
	Living organisms must increase the entropy of their surroundings.

	chemical and electrical gradients
	mechanical energy
	heat
	kinetic energy
	chemical energy

	The aerobic respiration of one molecule of glucose produces six molecules each of carbon dioxide and water.
	All types of cellular respiration produce ATP.
	Cellular respiration releases some energy as heat.
	The first and second choices are correct.
	The first, second, and third choices are correct.

	Energy conversions increase the order in the universe.
	The total amount of energy in the universe is constant.
	The decrease in entropy associated with life must be compensated for by an increase in entropy in the environment that life occurs in.
	The entropy of the universe is constantly decreasing.
	All reactions produce some heat.

	The entropy of the organism's environment must also be decreasing.
	Heat is being used by the organism as a source of energy.
	The first law of thermodynamics is being violated.
	Energy input into the organism must be occurring in order to drive the decrease in entropy.
	In this situation, the second law of thermodynamics must not apply.

	a sugar molecule
	an amino acid molecule
	a starch molecule
	a fatty acid molecule
	a cholesterol molecule

	DG
	DH
	DS
	TDS
	All of these values reveal the direction in which a reaction will go.

	DG is negative
	DG is positive
	DH is negative
	DH is positive
	DS is negative

	An input of free energy is needed.
	DG is positive.
	DH is negative.
	DS is positive.
	DS is negative.

	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
	increasing the temperature of a system will increase the probability of spontaneous change
	The first and second choices are correct.
	The first three choices are correct.

	The DH of the reaction must be negative.
	The DS of the reaction must be positive.
	The reaction must be endergonic.
	The difference between DH and TDS must be negative.
	All of the above are true.

	occurs only when an enzyme or other catalyst is present
	cannot occur outside of a living cell
	releases energy when proceeding in the forward direction
	is common in anabolic pathways
	leads to a decrease in the entropy of the universe

	HCl ® H+ + Cl-
	C6H12O6 + 6 O2 ® 6 CO2 + 6 H2O
	ATP ® ADP + Pi
	glucose + fructose ® sucrose
	all of the above

	the continuous removal of the products of a pathway to be used in other reactions
	an input of free energy from outside the pathway
	an input of heat from the environment
	The first and second choices are correct.
	The first, second, and third choices are correct.

	mechanical work, such as the beating of cilia
	transport work, such as the active transport of an ion into a cell
	chemical work, such as the synthesis of new protein
	the production of heat, which raises the temperature of the cell
	all of the above

	changing to ADP and phosphate
	releasing free energy that can be coupled to other reactions
	releasing heat
	acting as a catalyst
	lowering the free energy of the reaction

	ATP is acting as a transport protein to facilitate the movement of the ion across the plasma membrane.
	The hydrolysis of ATP is an endergonic reaction, and the active transport is an exergonic reaction.
	Neither of these reactions is spontaneous.
	This is an example of energy coupling.
	Both reactions are spontaneous because they result in an increase in entropy of the system.

	the RNA nucleotide adenosine
	the amino acid tryptophan
	the DNA nucleotide adenosine
	the nitrogenous base adenine
	the monosaccharide ribose

	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
	they are hydrogen bonds, which are only about 10% as strong as covalent bonds
	the phosphate groups are polar and are attracted to the water in the cell's interior
	the bonds between the phosphate groups are unusually strong and breaking them releases free energy

	Cells are less efficient at energy metabolism than reactions that are optimized in a test tube.
	The amount of heat released by a reaction has nothing to do with the free energy change of the reaction.
	In the cell, the hydrolysis of ATP is coupled to other endergonic reactions.
	In cells, ATP is hydrolyzed to ADP and Pi, but in the test tube it is hydrolyzed to carbon dioxide and water.
	Cells have the ability to store heat; this cannot happen in a test tube.

	The release of free energy during the hydrolysis of ATP heats the surrounding environment.
	The free energy released by ATP hydrolysis may be coupled to an endergonic process via the formation of a phosphorylated intermediate.
	It is catabolized to carbon dioxide and water.
	The DG associated with its hydrolysis is positive.
	The charge on the phosphate group of ATP tends to make the molecule very water-soluble.

	the conversion of glucose + fructose to make sucrose
	the contraction of a muscle cell
	the hydrolysis of ATP
	the active transport of a phosphate ion into the cell
	the formation of ATP from ADP + Pi

	activation energy is required
	the products are less complex than the reactants
	activation energy exceeds net energy release
	the potential energy of the products is less than the potential energy of the reactants
	it absorbs more energy

	The sign determines whether the reaction is spontaneous, and the magnitude determines the speed.
	The sign does not matter, but the larger the magnitude of DG the faster the reaction.
	The sign does not matter, but the smaller the magnitude of DG the faster the reaction.
	The more negative the DG, the faster the reaction is.
	Neither the sign nor the magnitude of DG have anything to do with the speed of a reaction.

	providing energy to speed up the rate of the reaction
	lowering the energy of activation for a reaction
	changing the direction of thermodynamic equilibrium
	changing endergonic into exergonic reactions
	lowering the free energy change of a reaction

	Enzymes increase the rate of a reaction by raising the activation energy for reactions.
	Enzymes react with their substrate (form chemical bonds) forming an enzyme-substrate complex, which irreversibly alters the enzyme.
	Enzymes speed up the rate of the reaction without changing the DG for the reaction.
	The most efficient enzymes can catalyze reactions in either direction.
	The more heat that is added to a reaction, the faster the enzymes will function.

	Enzymes can greatly speed up reactions, but they cannot change the net energy output because they cannot change the activation energy.
	Enzymes can change the equilibrium point of reactions, but they cannot speed up reactions because they cannot change the net energy output.
	Enzymes can greatly speed up reactions, but they cannot change the activation energy 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.
	None of the above is correct.

	the hydrogen bonds that define the structure of the enzyme's active site are unstable
	the substrate becomes a competitive inhibitor at lower temperature
	the enzyme was denatured
	the cofactors required by the enzyme system lack the thermal energy required to activate the enzyme
	there is too little activation energy available

	Most enzymes are proteins.
	An enzyme is not consumed by the catalytic process.
	An enzyme is very specific in terms of which substrate it binds to.
	An enzyme lowers the activation energy of a chemical reaction.
	All of the above are correct statements about enzymes.

	The active site has a fixed structure (shape).
	Coenzymes are never found in the active site of an enzyme.
	The active site may resemble a groove or pocket in the surface of a protein into which the substrate fits.
	The structure of the active site is not affected by changes in temperature.
	The active site allows the reaction to occur under the same environmental conditions as the reaction without the enzyme.

	The substrate can be altered so that it is induced to fit into the enzyme's active site.
	The enzyme structure is altered so that it can be induced to fit many different types of substrate.
	The presence of the substrate in solution induces the enzyme to slightly change its structure.
	The shape of the active site is nearly perfect for specifically binding the enzyme's substrate(s).
	The enzyme changes its shape slightly as the substrate binds to it.

	Heat from the environment is necessary for substrates to get over the activation energy barrier.
	Increasing temperature increases the kinetic energy of the substrates.
	Increasing the temperature will increase the rate of enzyme-catalyzed reactions.
	The first and second choices are correct.
	The first, second, and third choices are correct.

	an increase in concentration of enzyme
	increasing the temperature by a few degrees
	increasing the substrate concentration
	The first and second choices are correct.
	The first, second, and third choices are correct.

	heating the enzyme
	cooling the enzyme
	substrate concentration
	pH
	all of the above

	most substrates don't function well at high or low pH
	high or low pH may disrupt hydrogen bonding or ionic interactions and thus change the shape of the active site
	low pH will denature all enzymes
	changes in pH can cause loss of cofactors from the enzyme
	the binding of hydrogen ions to the enzyme absorbs energy and thus there may not be enough energy to overcome the activation energy barrier

	A competitive inhibitor binds to the enzyme at a place that is separate from the active site.
	The action of competitive inhibitors may be reversible or irreversible.
	A noncompetitive inhibitor does not change the shape of the active site.
	When the product of an enzyme or an enzyme sequence acts as its inhibitor, this is known as positive feedback.
	Inhibition of enzyme function by compounds that are not substrates is something that only occurs under controlled conditions in the laboratory.

	Succinylcholine must be a competitive inhibitor with acetylcholine.
	Succinylcholine must be an allosteric regulator for this enzyme.
	The active site must have the wrong configuration to permit succinylcholine binding.
	Succinylcholine must be a non-competitive inhibitor.
	The activation energy barrier for succinylcholine hydrolysis is higher than for acetylcholine hydrolysis.

	feedback inhibition
	competitive inhibition
	allosteric regulation
	non-competitive inhibition
	cooperativity

	They are sensitive to environmental conditions.
	They are acted on by inhibitors.
	They exist in active and inactive conformations.
	They can bind to a range of substrates.
	All of the above statements are true of allosteric proteins.

	The allosteric inhibitor binds to the active site, preventing the substrate from binding.
	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.
	The allosteric inhibitor lowers the temperature of the active site.
	The allosteric inhibitor binds to the substrate and prevents it from binding at the active site.

	High levels of ADP act as an allosteric inhibitor of catabolic pathways.
	High levels of ATP act as an allosteric activator of anabolic pathways.
	High levels of ATP act as an allosteric activator of catabolic pathways.
	High levels of ADP act as an allosteric activator of catabolic pathways
	High levels of ADP act as an allosteric inhibitor of anabolic pathways.