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64 Cards in this Set

  • Front
  • Back
What is the first law of thermodynamics?
the law of conservation of energy - Energy can neither be created nor destroyed.
Despite the first law of thermodynamics, energy can be...
transduced - converted from one form of energy to another

Cells are also capable of transduction.
Regardless of the transduction process, the total amount of energy in the universe is _____________.
constant
What is the most important energy transduction in the biological world which converts sunlight into chemical energy?
photosynthesis - provides the fuel that directly or indirectly powers nearly all the activities of life forms
What does the enzyme luciferase in fireflies enable these organisms to do?
convert chemical energy back into light (reverse photosynthesis)
Reactions that lose heat are ________________.
exothermic
Reactions that gain heat are ________________.
endothermic
What is the second law of thermodynamics?
Events in the universe have direction; they tend to proceed in a "downhill" fashion, going from a higher to lower state of energy
What is the term that describes events that are thermodynamically favorable and can occur without the input of external energy?
spontaneous
Loss of energy during a process is the result of a tendency for ___________________ to increase whenever there is a transfer of energy.
randomness (entropy)
Every event is accompanied an increase in the ______________ of the universe.
entropy
Spontaneity depends on both ___________ and _____________.
entropy - randomness or disorder AND enthalpy - total energy content of the system
All chemical reactions spontaneously proceed toward the _________________.
equilibrium
The release of heat is an example of an ______________ in entropy.
increase
Together, what do the first and second laws of thermodynamics indicate?
The energy of the free universe is constant, but the entropy continues to increase toward a maximum.
All spontaneous energy transformations must have a _________________ delta G.
negative - the process must proceed toward a lower state of free energy
What are processes that occur spontaneously, thermodynamically favored, and have a negative delta G described as?
exergonic
All nonspontaneous energy transformations must have a _______________ delta G.
positive
What are processes that occur nonspontaneously, thermodynamically unfavorable, and have a positive delta G described as?
endergonic
All _________ reactions are coupled reactions.
ATP

Coupling is a major way to get around energy requirements. One gives off energy, and the paired reaction is right there to absorb it.
The greater the delta G, the farther the reaction is from equilibrium. This means..
more work can be performed by the system
When delta G is 0, the reaction is...
at equilibrium and no further work can be obtained
The delta G of ATP hydrolysis is -7.3 kcal/mol. This suggests that..
the ATP hydrolysis reaction is a highly favorable (exergonic) reaction
Why is ATP used to drive most endergonic processes within the cell?
because its terminal phosphate group can be transferred to a variety of different types of molecules, including amino acids, sugars, lipids, and proteins.

In most coupled reactions, the phosphate group is transferred in an initial step from ATP to one of these acceptors and is subsequently removed in the second step.
What may energy from ATP hydrolysis be used do within a cell?
separate charge across a membrane

concentrate a particular solute within the cell

drive an unfavorable chemical reaction

slide filaments across one another (shortening of a muscle cell)

donate a phosphate to a protein (added phosphates become binding sites for these proteins)
Why can cellular metabolism maintain itself at irreversible, nonequilibrium conditions?
The basic principles of thermodynamics were built upon nonliving, closed systems (no exchange of matter between the system and surroundings).

Unlike the environment within a test tube, the cell is an open system.

The continual flow of oxygen and other materials in and out of our cells allows cellular metabolism to exist at a steady state.
Maintaining a steady state requires a constant input of energy, while maintaining ______________ does not.
equilibrium
In a steady state, the concentrations of reactants and products remain _____________ but..
constant but not at equilibrium
What is the term used to describe biological catalysts (usually proteins) that speed up chemical reactions?
enzymes
_______________ are the mediators of metabolism, responsible for virtually every reaction in the cell.
Enzymes
Without, ______________ metabolic reactions would proceed so slowly as to be imperceptible.
enzymes
________________ is a protein catalyst, while ________________ is an RNA catalyst.
enzyme - protein
ribozyme - RNA
List the properties of enzymes.
exist in small amounts

are not altered irreversibly (same enzyme can be used repeatedly in different reactions)

have no effect on the thermodynamics of the reaction, just the rate
Enzymes do not supply energy for a chemical reaction, therefore...
they cannot determine whether a reaction is thermodynamically favorable or unfavorable
What is the term used to describe the reactants bound by an enzyme?
substrates - enzymes are highly specific for their substrates
Chemical transformations require that certain covalent bonds be broken within the reactants. For this to occur, the reaction must overcome a barrier. What is this amount of energy required called?
activation energy (Ea) - small energy input that is required for any chemical transformation
How does the Ea barrier affect the process of thermodynamically unstable reactions?
it slows the process
When reactant molecules reach the peak of the Ea barrier, what is this called?
transition state
What helps molecules reach the transition state due to the decrease of required activation energy?
enzymes
How are enzymes able to lower activation energies?
by binding more tightly to the transition state than to the reactants, which stabilizes this activated complex, and decreases its energy
How does heat increase the rate of a reaction?
by increasing the content of the molecules
What portion of the enzyme does the substrate bind to?
active site

The active site and substrate have complementary shapes that allow substrate specificity.
What is the term that describes the physical association between an enzyme and its substrate during which catalysis of the reaction takes place?
enzyme-substrate complex - forms once everything is bound
The active site is typically buried in a cleft or crevice that leads from the aqueous surroundings into the depths of the protein. Active sites are often thought of as...
pockets in the enzyme
substrates = ______________
reactants
structure = _____________
function
What are the three ways in which enzymes accelerate reactions?
maintaining precise orientation (holding on tightly to substrate)

changing substrate reactivity by altering electrostatic configuration

exerting physical stress on bonds in the substrate to be broken
Shifts in the conformation after binding cause ____________________ between the enzyme and substrate.
induced fit - complementary fit that moves the proper reactive groups of the enzyme into place (strain is relieved)
At saturation, every enzyme is working at ________________________.
maximum velocity
Enzyme inhibitors _________ the rates for enzymatic reactions.
slow
What is the difference between reversible and irreversible inhibitors?
Reversible inhibitors bind loosely to the enzyme, whereas irreversible inhibitors (suicide inhibitors) bind tightly to the enzyme.
Competitive inhibitors compete with the ______________ for a binding site on the enzyme.
substrate

resemble the substrate, can be overcome with high substrate inhibitor ratios
What is the difference between competitive inhibitors and noncompetitive inhibitors?
Competitive inhibitors compete with the substrate to bind to the active site of the enzyme, whereas noncompetitive inhibitors bind to other areas besides the active site and INACTIVATE the enzyme.

Noncompetitive inhibitors (allosteric inhibitors) cannot be overcome with high substrate inhibitor ratios as competitive inhibitors can.
Enzymes reduce enzyme efficiency. Competitive inhibitors _____________ Km but ______________ Vmax.
Competitive inhibitors increase Km but do not change Vmax.
Enzymes reduce enzyme efficiency. Noncompetitive inhibitors ______________ Km but ______________ Vmax.
Noncompetitive inhibitors do not change Km but decrease Vmax.
Which reactions break down complex substrates into simple end products?
catabolic pathways (energetically unfavorable) - provide raw materials for the cell, provide chemical energy for the cell
Which reactions synthesize complex end products from simple substrates?
anabolic pathways (energetically favorable) - require energy, use ATP and NADPH from catabolic pathways
Which stage of metabolism consists of macromolecules being hydrolyzed into their building blocks?
stage 1
Which stage of metabolism consists of building blocks being degraded into a few common metabolites?
stage 2
Which stage of metabolism consists of small molecular weight metabolites like acetyl-CoA being degraded and yielding ATP?
stage 3
What is the first stage in the catabolism of glucose that occurs in the soluble portion of the cytoplasm?
glycolysis
What is the second stage in the catabolism of glucose that occurs in the mitochondria of eukaryotic cells?
tricarboxylic cycle (TCA, Krebs cycle)
All cells perform glycolysis, while the Krebs cycle is unique to _________________ cells.
eukaryotic
Which reactions of glycolysis are NOT at or near equilibrium?
those catalyzed by hexokinase, phosphofructokinase, and pyruvate kinase

Only these three steps require ATP.