L5 Energy Flashcards

1
Q

What is metabolism?

A

Metabolism comprises all chemical reactions in a cell

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2
Q

What two types of reactions can metabolism be divided into?

A

Anabolic and catabolic reactions

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3
Q

What are anabolic reactions? (2)

A
  • Anabolic reactions link simple molecules together
  • They are energy storing reactions; they require energy
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4
Q

What are examples of anabolic reactions (3)

A
  • DNA replication
  • protein synthesis
  • making of starch
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5
Q

What are catabolic reactions (2)

A
  • They break down complex molecules into simpler ones
  • They release energy
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6
Q

What is an example of a catabolic reaction?

A

digestion of food

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7
Q

What is the def of energy?

A

energy is defined as the potential capacity to do work w

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8
Q

What drives energy conversions?

A

The tendency of energy to become evenly distributed or dispersed over time (2nd law of thermodynamics)

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9
Q

What is the first law of thermodynamics?

A

Energy is neither created nor destroyed

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10
Q

What is the second law of thermodynamics

A

Energy spontaneously disperses from being localized to becoming spread out if it is not hindered from doing so
→ energy moves from high energy area to low energy area

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11
Q

What are examples of the second law of thermodynamics? (3)

A
  • a hot cup of coffee will cool down, but never warm up on its own
  • a balloon will lose air, but never gain it on its own
  • a swimmer can dive into the water but is never thrown out of the water by concerted movement of water molecules
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12
Q

What happens to entropy (disorder) as energy follows the second law of thermodynamics?

A

Disorder increases

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13
Q

What is ΔG

A

Free energy

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14
Q

How can cells release free energy? (2)

A
  1. with a chemical reaction creating disorder (entropy aka ΔS)
  2. with a chemical reaction releasing heat (enthalpy aka ΔH)
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15
Q

What is the equation that expresses the change in free energy

A

ΔG = ΔH - TΔS

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16
Q

What does it mean when ΔG is negative?

A
  • Energy is released/dispersed
  • The reaction is favorable, it can happen spontaneously
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17
Q

What does it mean when ΔG is positive?

A

Energy is required for the reaction to happen

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18
Q

REACTION 1:
Heat is released (neg ΔH) and disorder increases (pos TΔS)
What does this mean for free energy?

A
  • This reaction is always spontaneous (exergonic) because ΔG is always negative
  • (-)ΔH - TΔS = (-)ΔG
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19
Q

REACTION 2:
Heat is released (neg ΔH) and disorder decreases (neg TΔS)
What does this mean for free energy?

A
  • ΔG is only negative under a certain temperature, so the rx is only spontaneous under that T
  • (-)ΔH - (-)TΔS = -ΔH +TΔS
  • An example of this reaction is in protein folding: this process can only occur below a certain temperature
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20
Q

REACTION 3:
Heat is used (pos ΔH) and disorder increases (pos TΔS)
What does this mean for free energy?

A
  • (+)ΔH - (-)TΔS
  • The reaction is spontaneous above a certain temperature
  • An example of this is dissolving NaCl in water
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21
Q

REACTION 4:
Heat is used (pos ΔH) and disorder decreases (neg TΔS)
What does this mean for free energy?

A
  • never spontaneous (endergonic)
  • (+)ΔH - (-)TΔS = (+) ΔG
  • this applies to most anabolic reactions
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22
Q

How can anabolic reactions occur? (reactions with a positive ΔG

A

They can ONLY occur when they are coupled to a exergonic reaction to make the overall ΔG negative

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23
Q

What happens when you increase the amount of reactants in a reversible reaction?

A

You speed up the forward reaction

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24
Q

What happens when you increase the amount of products in a reversible reaction?

A

You speed up the reverse reaction

25
Q

What happens when you leave a reversible reaction alone?

A

It will proceed to the point of chemical equilibrium, where no more net changes take place

26
Q

What happens to the speed of the forward and reverse reactions when there is chemical equilibrium?

A

They proceed at the same rate from one another

27
Q

What happens to ΔG at the point of chemical equilibrium?

A

ΔG = 0

28
Q

What is ATP?

A

ATP is Adenosine triphosphate
It is a molecule; an organic compound

29
Q

What do cells use ATP for?

A

To capture, transfer and store energy

30
Q

How is ATP used to allow for endergonic reactions?

A

Some of the free energy released by exergonic reactions is capture in ATP, which then can drive endergonic reactions

31
Q

What type of reaction is ATP hydrolysis (endergonic or exergonic)

A

Exeregonic

32
Q

What can ATP hydrolysis be used for?

A

It can be used to drive endergonic reactions such as making a polymer

33
Q

What is the reaction of ATP hydrolysis?

A

ATP + H2O → ADP + Pi + free energy
(Pi = phosphate ion)

34
Q

Why is ATP hydrolysis so exergonic?

A

Because the resulting ADP from this reaction is constantly removed either by reforming ATP or by hydrolysis to AMP

35
Q

Can you know the rate of a reaction knowing that ΔG is negative?

A

No you cannot predict the rate of the reaction

36
Q

At what rate do most exergonic reactions occur? (slow or fast)

A

Most occur at an immeasurable slow rate

37
Q

What do exerfonix reactions need to get started?

A

They need a bit of activation energy to get started, to put the molecules into a transition state favorable to the reaction

38
Q

What is a catalyst?

A

A catalyst is any substance that speeds up a chemical reaction without itself being used up

39
Q

Can catalysts speed up all types of reactions?

A

No, catalysts can only speed up spontaneous reactions (reactions where ΔG is negative)

40
Q

Can catalysts change the value of ΔG?

A

No

41
Q

What are most biological catalysts?

A

Most biological catalysts are proteins called enzymes

42
Q

What can biological catalysts (enzymes) also be called?

A

Sometimes they are called RNAs that have folded into a 3D structure, especially within the ribosome.

43
Q

How do enzymes work?

A

Enzymes work by lowering the activation energy

44
Q

Why are enzymes crucial in our body?

A
  • Because at 37 degrees, most spontaneous reactions do not proceed since the energy barrier cant be overcome.
  • So, since enzymes can lower the activation energy, they are important to our bodies
45
Q

What happens when reactants (called substrate) binds to the active site of the enzyme?

A

The enzyme often undergoes a small conformational change (a shape change) which brings the substrates into a transition state

46
Q

What happens when the products leave the enzyme site?

A

The enzyme reverts to its og shape

47
Q

What does the enzyme do that induces the transition state? (3)

A
  • It can bind the substrates in the correct orientation
  • It can expose the reactants to altered charge environments that promote catalysis
  • It can induce a strain on the substrate that facilitates breaking of a covalent bond
48
Q

What are cofactors?

A

Cofactors are small organic molecules or ions that are not amino acids and are associate more or less tightly with the enzyme

49
Q

What are cofactors used for

A

Certain enzymes need cofactors in order to function

50
Q

When is an enzyme saturated?

A

When all active sites are occupied

51
Q

What happens if the substrate concentration increases when an enzyme is already saturated?

A

Nothing : A further increase in substrate concentration will no longer increase the rate of product formation

52
Q

What is the maximum speed of a reaction called?

A

The turnover rate

53
Q

What determines the turnover rate?

A

The speed of the reaction when the enzyme is saturated

54
Q

How much can the turnover rate vary?

A

It can vary from 1 molec/sec to 40 million molec/sec

55
Q

What is enzyme regulation?

A

The control of the rate of a reaction catalyzed by an enzyme by a regulatory molecule

56
Q

What are the 2 types of enzyme regulation?

A

Competitive inhibition and allosteric regulation

57
Q

What is competitive inhibition?

A

A regulatory molecule binds to the enzyme’s active site and because of this the substrates cannot bind anymore

58
Q

What is allosteric regulation?

A

A regulatory binds to a different site on the enzyme which changes the shape of the enzyme’s active site. The substrates can no longer bind to the active site.

59
Q

Which is more efficient: competitive inhibition or allosteric regulation? and why?

A
  • Allosteric inhibition is much more efficient because less inhibitor molecules are required.
  • You need more competitor molecules than substrate molecules for effective competitive inhibition, but you only need more allosteric regulators than enzymes, because nothing else binds at the allosteric site.