Ch. 8 Exam Flashcards

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1
Q

Define energy.

A

The capacity to cause change or perform work

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2
Q

Explain the two types of energy.

A
  • Kinetic energy: energy of motion
    • Movement
      -Heat: kinetic energy of molecular motion
    • In cells, molecules are broken to obtain kinetic energy
  • Potential energy: energy of position or configuration
    • In cells, potential energy is often stored in chemicals
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3
Q

Where do molecules store potential energy?

A

In chemicals

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4
Q

Explain the first law of thermodynamics.

A

Laws of thermodynamics govern energy conversions
- Matter and energy cannot be created or destroyed, and energy conversions increase entropy (disorder
- Molecules (fats and carbohydrates) store potential energy i their bonds (because electrons have potential energy

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5
Q

Explain the second law of thermodynamics.

A
  • In cells, some reactions release energy whereas others take up energy.
  • Free energy (deltaG) of a reaction is the amount of energy available to do work
  • Exothermic reaction: releases heat energy
    • Products have less potential energy than reactants
  • Endothermic reaction: Heat energy is taken up
    • Products have higher potential energy than reactants
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6
Q

During any energy conversion, some energy is “lost” as heat. Explain this phenomenon.

A
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7
Q

Define free energy.

A
  • Free energy (deltaG) of a reaction is the amount of energy available to do work
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8
Q

Compare and contrast exothermic and endothermic reactions.

A
  • Exothermic reaction: releases heat energy
    • Products have less potential energy than reactants
  • Endothermic reaction: Heat energy is taken up
    • Products have higher potential energy than reactants
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9
Q

When the concentration of reactants is high, ____ (more/less) collisions should occur, and reactions should proceed more _______ (quickly/slowly).

A
  • more
  • quickly
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10
Q

Explain how energetic coupling works.

A
  • Occurs between exergonic and endergonic reactions
  • This allows chemical energy released from one reaction to drive another reaction
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11
Q

What transfers in a reduction—oxidation (redox) reaction?

A
  • Chemical reactions that involve electron transfer
  • Protons (H+) usually accompany an electron during its transfer
  • Oxidation and reduction events are always coupled
    -If one atom loses an electron, another has to gain it
    • Electron donors are always paired with electron acceptors
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12
Q

(Not a question, just information!) Oxidation and reduction events are coupled. If one atom loses an electron, another had to gain it. Thus, electron donors are always paired up with electron acceptors to keep the exchange equal.

A
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13
Q

Define and explain reduction.

A
  • When an atom or molecule gains an electron
    • “adds Hs)
    • Occurs when molecules are assimilated
    • Increases potential energy
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14
Q

Define and explain oxidation.

A
  • When an atom or molecule loses an electron
    • “remove Hs)
    • Occurs when molecules are being broken up
    • Loses potential energy
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15
Q

During a redox reaction, electrons can be used for two different purposes. List those purposes.

A
  • Be transferred completely from one atom to another
  • Be used to form different covalent bonds
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16
Q

What is reduced to form NADH? What is NADH’s function?

A
  • Nicotinamide adenine dinucleotide (NAD+)
  • NADH is a high energy electron carrier that has the ability to acquire, then donate electrons to other molecules
17
Q

List three aspects of ATP (adenosine triphosphate).

A
  • Has high potential energy and is used for most cellular activities
  • Works by phosphorylating target molecules (transferring a PO4 3-)
  • Have high potential energy because negative charges in its 3 phosphate groups repel each other
18
Q

How does ATP work on target molecules?

A

Phosphorylating

19
Q

Why do the electrons in ATP have high potential energy?

A

Negative charges in its 3 phosphate groups repel each other

20
Q

What is ATP hydrolysis important for?

A

For transport contraction and energy for enzymes to catalyze chemical reactions

21
Q

Define enzyme. Why are they important?

A
  • Protein catalysts that facilitate specific chemical reactions within a cell
  • Important because they speed up chemical reactions that are required for life
22
Q

Define and explain anabolism. Is anabolism endergonic or exergonic?

A
  • Refers to chemical reactions that build smaller molecules into larger molecules
    • Dehydration reactions
    • Endergonic
      • They require an input of energy
      • The larger product molecules are more ordered and therefore have more potential energy than the smaller reactant molecules
23
Q

Define and explain catabolism. Is catabolism endergonic or exergonic?

A
  • Refers to chemical reactions that break down larger molecules into smaller molecules
    -Hydrolysis
  • exergonic
    • They release energy
    • The smaller products molecules are less ordered and therefor have less potential energy than the larger reactant molecules
  • Although catabolic reactions are exergonic, they do not occur spontaneously
24
Q

Where do substrates bind in an enzyme?

A

Active site

25
Q

Define the conformational change that enzymes undergo when the substrate are bound to the enzyme.

A

Induced fit

26
Q

Define activation energy (Ea).

A
  • The energy required by reactant molecules to get the reaction started (activated).
    • Energy is required to weaken the chemical bonds of the reactants
27
Q

How do enzymes catalyze chemical reactions? Meaning: how do they speed reactions along?

A
  • By lowering the amount of activation energy required
    • Enzymes make it easier to break the reactants’ chemical bonds
28
Q

List and explain the three steps of enzyme catalysis.

A
  1. Initiation: Substrates are precisely oriented as they bind to the active site
  2. Transition state facilitation: Interactions between the substrate and active site of enzyme (lowering Ea)
  3. Termination: Reaction products have a lower affinity to active site and, therefore released
29
Q

Are enzymes used only once before degradation, or multiple times?

A
30
Q

How are enzymes named? Give an example.

A
  • Enzymes are named for the substrate (reactant) molecules on which they act
    • Enzymes generally have an ase suffix
  • The enzyme sucrase catalyzes the hydrolysis of sucrose into glucose and fructose
31
Q

There are three factors that affect the rate of enzyme activity. Explain the first: substrate concentration, and how it affects the rate of enzyme activity.

A
  • Enzyme activity increases as substrate concentration increases
  • At very high substrate concentrations, all of the enzyme’s active sites are occupied by substrate
    • Enzymes activity cannot increase any further
32
Q

The second factor affecting the rate of enzyme activity is temperature. Explain how temperature affects the rate of enzyme activity.

A
  • Enzyme activity increases as temperature increases
  • At extremely high temperatures, enzyme activity decreases as the enzyme becomes denatured
33
Q

The third and final factor affecting the rate of enzyme activity is pH. Explain how pH affects the rate of enzyme activity.

A
  • Each enzyme has an optimal pH at which activity is maximized
  • A much lower or higher pH can cause enzyme to denature because they operate at an optimal pH
34
Q

List and describe the three molecules/atoms that assist enzymes.

A
  • Coenzymes: non-protein organic molecules that aid enzyme function
    • Vitamins
  • Cofactors: Inorganic ions that aid enzyme function
    • Minerals
  • Functional groups: sometimes a function group must be added or removed for enzyme function
    • Phosphorylation
35
Q

Define and explain competitive inhibitors. Specifically: where do they bind to an enzyme?

A
  • Molecules that have a shape similar to the enzymes substrate
    • They bind to the active site and block the binding of the substrate
    • No chemical reaction occurs
36
Q

Define and explain noncompetitive inhibitors. Specifically: where do they bind to an enzyme?

A
  • They bind to a site other than the active site called the allosteric site
    • Binding at the allosteric site alters configuration of the enzymes, ultimately interfering with the ability of the substrate to interact with the active site of the enzyme
    • The enzyme and substrate shapes no longer match
    • No chemical reaction occurs
37
Q

Define and explain allosteric activation. Specifically: where do they bind to an enzyme?

A
  • Some molecules called inducers interact with the allosteric site of an enzyme changing its configuration
  • Rather than deactivating the enzyme, they activate it
38
Q

When does feedback inhibition occur? When are pathways shut down?

A
  • Occurs when an anthem in a pathway is inhibited
  • By the final product of that pathway
  • Pathway can shut down when
    • Products are no longer needed by the cell