Explore the fundamentals of metabolism in 'Chapter 6: An Introduction to Metabolism'. This quiz assesses understanding of energy transformations, the laws of thermodynamics, and how organisms interact with their environment energetically. Essential for students of biochemistry and related fields.
Deals with entropy
States that energy is neither created nor destroyed
Deals with heat content
States that entropy spontaneously increases
Predicts the direction of a reaction
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Electrical energy
Mechanical energy
Electromagnetic energy
Kinetic energy
Chemical energy
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The metabolism of an organism is isolated from its surroundings
Organisms can reverse the increase in entropy
Organisms acquire energy from their surroundings
Organisms are capable of circumventing the second law of thermodynamics
Because energy is conserved, organisms do not require energy input from their surroundings
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Endergonic
Exergonic
Exothermic
Endothermic
Enthalpic
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To create an energy barrier between substrates
To lower the energy of the activation of a reaction
To change the direction of thermodynamic equilibrium
To change endergonic into exergonic reactions
To allow substrates to move more freely in solution
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It states that energy is neither created nor destroyed.
It deals with entropy.
It deals with heat content.
It deals with spontaneity.
All the above are true.
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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 noncompetitive inhibitor
The activation energy barrier for succinylcholine hydrolysis is higher than for acetylcholine hydrolysis
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They are sensitive to environmental conditions.
They are acted on by inhibitors.
They exist in active and inactive conformations.
They have more than one subunit.
All of the above statements are true of allosteric proteins.
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Heating the enzyme
Cooling the enzyme
Salt concentration
PH
All of the above can affect enzyme activity.
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The burning of gasoline in a car engine
The production of sugar by photosynthesis
The production of electrical power by damming a river
Cracking a nut by using a nutcracker
Plugging a stereo into a wall socket to play music
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Most enzymes are proteins
An enzyme is not consumed by the catalytic process.
An enzyme is very specific in terms of which substrates it can bind to.
An enzyme lowers the activation energy of a chemical reaction.
All of the above.
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Occurs only when an enzyme is present
Occurs within living cells but not in a test tube
Releases energy when proceeding in the forward direction
Occurs in all living cells
All of the above
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The RNA nucleotide adenosine
The amino acid tryptophan
The DNA nucleotide adenosine
Cholesterol
The monosaccharide galactose
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The DG of the reaction must be negative.
The reaction must be exergonic.
The environment has adequate thermal energy to meet the activation energy requirement.
The bonds must have absorbed enough energy to become unstable.
All of the above are true.
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Activation energy is necessary
No kinetic energy is released
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
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The release of free energy during the hydrolysis of ATP heats the surrounding environment.
Its free energy is 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 polar phosphate groups assist in the alignment of polar substrates as they enter an enzyme's active site.
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Greatly speed up reactions ... change the net energy output ... change the activation energy
Change the equilibrium point of reactions ... speed up reactions ... change the net energy output
Greatly speed up reactions ... change the activation energy ... change the net energy output
Lower the activation energy of reactions ... change the equilibrium point ... change the net energy output
None of the above
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HCl —> H+ + Cl-
C6H12O6 + 6 O2 —> 6 CO2 + 6 H2O
ATP —> ADP + Pi
Maltose + fructose —> sucrose
All of the above
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The aerobic respiration of glucose generates heat.
All types of cellular respiration produce ATP.
CO2 is exhaled as a by-product of aerobic respiration.
Photosynthesis enables plants to create energy from sunlight.
Energy is stored during the Calvin cycle.
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DG
DH
DS
TDS
All of these values tell us the direction in which a reaction will go.
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A competitive inhibitor binds to the enzyme outside 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.
Antibiotics and pesticides generally do not act on enzymes, but rather affect the genetic code of their victims.
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Energy conversions increase the order in the universe.
The total amount of energy in the universe is constant.
The ordering of one system depends on the disordering of another.
The entropy of the universe is constantly decreasing.
All reactions produce some heat.
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Changing to ADP and phosphate
Transferring a phosphate group to some other molecule
Releasing heat
Acting as a catalyst
Lowering the free energy of the reaction
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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 capacity of a system to perform work is related to the total energy of the system
All of the above are true
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A sugar molecule
An amino acid molecule
A starch molecule
A fatty acid molecule
A cholesterol molecule
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Mechanical work, such as the beating of cilia,
Transport work, such as the movement of glucose into an adipose cell,
Chemical work, such as the synthesis of new protein,
Mechanical work, such as pumping blood through the circulatory system,
All of the above
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The substrate can be altered so it is induced to fit into the enzyme's active site.
The enzyme is altered so it is induced to fit many different types of substrate.
Several sites on an enzyme can be induced to act on a substrate.
The enzyme changes its shape slightly as it binds to the substrate.
All of the above.
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The sun's energy is being captured by photosynthesis
Heat is being used by organisms as a source of energy
The first law of thermodynamics is being violated
Energy input will be needed to maintain organization
The amount of usable energy in the system is increasing
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Has a rigid shape, which does not change
Is where the coenzyme will never be found
Resembles a groove or crevice into which the substrate fits
Is the place where both apoenzymes join
Fits the substrate as a lock and key
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Enzymes raise the activation energy for reactions.
Enzymes react with substrates (form chemical bonds) to form an enzyme-substrate complex, which irreversibly alters the enzyme
Most enzymes are chains of amino acids.
Only the most efficient enzymes can catalyze reactions in either direction.
The more a reaction is heated, the faster the enzymes will function.
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Most substrates don't function well at high or low pH
High or low pH may disrupt hydrogen bonding and change the shape of the active site
High or low pH may cause the active site to lose its energy
Excess hydrogen ions can combine with the substrate and cause the reaction to go more slowly
Hydrogen ions absorb energy and thus there may not be enough energy to get the reaction started.
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Feedback inhibition
Competitive inhibition
Allosteric regulation
The participation of a co-factor
Cooperativity
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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
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
All of the above
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Allosteric activation
Allosteric inhibition
Competitive inhibition
Cooperativity
Feedback inhibition
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The hydrogen bonds that define the enzyme's active site are unstable
The substrate becomes an allosteric regulator
The enzyme was denatured
The co-factors required by the enzyme system lack the thermal energy required to activate the enzyme
There is too little activation energy available
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Product ... active site
Product ... allosteric site
Substrate ... active site
Substrate ... allosteric site
Substrate ... active site and allosteric site
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Outside energy is needed.
DG is positive.
DH is negative
DS is positive.
DS is negative
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ATP —> ATP + Pi
ADP —> ATP + Pi
ATP —> ADP
ADP —> ATP
ADP + Pi —> ATP
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DG is negative
DG is positive
DH is negative
DH is positive
TDS is negative
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