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Biology > Chapter 6: Metabolism > Flashcards

Chapter 6: Metabolism Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

bioenergetics

A

study of energy flowing through living systems

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2
Q

metabolism

A

all the chemical reactions that happen inside of cells

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3
Q

metabolic pathway

A

series of biochemical reactions that convert a substrate into its final product

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4
Q

What are the two main metabolic pathways?

A

Anabolic and catabolic

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5
Q

anabolic pathway

A

synthesises complex molecules from simple ones

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6
Q

catabolic pathway

A

breaks down complex molecules into simple ones

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7
Q

kinetic energy

A

energy an object has when in motion

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8
Q

potential energy

A

energy an object has when it has a potential to do work

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9
Q

chemical energy

A

potential energy that exists between molecular bonds

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10
Q

Gibbs free energy

A

refers to the usable energy in a chemical reaction after entropy is taken into account

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11
Q

delta G

A

change in free energy

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12
Q

delta S

A

energy lost to entropy

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13
Q

delta H

A

total energy change in a system

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14
Q

enthalpy

A

total energy change in a system

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15
Q

What is the formula for calculating the change in free energy?

A

ΔG = ΔH − TΔS

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16
Q

What does ‘T’ represent in ΔG = ΔH − TΔS?

A

absolute temperature in Kelvin

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17
Q

What units express change in free energy?

A

Amount of energy (in kilojoules or kilocalories) per mole of reaction product under standard conditons

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18
Q

What is the conversion rate for kilocalories to kilojoules?

A

1 kcal = 4.184 kJ

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19
Q

What are the factors for standard conditions for calculating free energy?

A

Standard pH, temperature and pressure

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20
Q

What is the standard pH value?

A

pH 7

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21
Q

What is the standard temperature value?

A

25 degrees Celsius

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22
Q

What is the standard pressure value?

A

100 kilopascals

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23
Q

How much pressure is 1 atmosphere?

A

100 kilopascals

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24
Q

What will the value delta G be if energy is released in a reaction?

A

It will be negative

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25
Q

exergonic reaction

A

reaction that releases free energy

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26
Q

Are exergonic reactions spontaneous?

A

Yes, they require no energy input

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27
Q

endergonic reaction

A

reaction that results in a gain of free energy

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28
Q

Are endergonic reactions spontaneous?

A

No, they require an energy input to happen

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29
Q

chemical equilibrium

A

when there is no net change in amount of reactants and products in a chemical reaction

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30
Q

In what condition is there the lowest amount of free energy and maximal entropy?

A

In equilibrium

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31
Q

What would happen if a cell was in a closed environment?

A

Its chemical reactions would reach equilibrium and it would run out of energy and die

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32
Q

Do chemical reactions in a cell ever reach equilibrium?

A

No, they move towards equilibrium but never reach it

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33
Q

Why do cells never reach equilibrium?

A

They are in an open environment and materials are constantly being moved in and out

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34
Q

activation energy

A

energy necessary to start a reaction

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35
Q

What is activation energy abbreviated to?

A

EvA

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36
Q

transition state

A

high-energy, unstable form between the substrate and product

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37
Q

Why do exergonic reactions need energy to start?

A

Reactants must be slightly contorted first for bonds to break and need energy to reach this state of contortment

38
Q

Where does the activation energy for a reaction come from?

A

From the heat in the surrounding area

39
Q

How does heat energy provide the activation energy for a reaction?

A

When the reactants absorb enough heat, they will reach the transition state and the reaction will occur

40
Q

How does amount of activation energy needed affect the rate of reaction?

A

The greater the activation energy, the slower the reaction

41
Q

Why are catalysts important in chemical reactions?

A

They lower the activation energy required and prevent the body from producing too much heat to overcome the original activation energy

42
Q

What does the first law of thermodynamics state?

A

Energy cannot be created or destroyed

43
Q

What does the second law of thermodynamics state?

A

The total entropy of the universe is always increasing

44
Q

entropy

A

the measure of disorder in a system

45
Q

What is the relationship between entropy and energy

A

High entropy means low energy

46
Q

nucleoside

A

a nitrogenous base attached to a sugar

47
Q

adenosine

A

nucleoside made of adenine and ribose

48
Q

How are the phosphate groups in ATP named?

A

In order of closest to furthest from the ribose sugar, they are named alpha, beta and gamma

49
Q

Where are the high-energy bonds in ATP located?

A

Between the gamma and beta phosphate, and the beta and alpha phospahte

50
Q

phosphoanhydride bond

A

high-energy bonds that hold together the phosphate groups in ATP

51
Q

How is ATP converted to ADP?

A

Through hydrolysis

52
Q

How is an inorganic phosphate group as a chemical formula?

A

Pi

53
Q

What is the chemical equation for ATP being converted into ADP?

A

ATP + H20 -> ADP + Pi + free energy

54
Q

Is the conversion of ATP into ADP reversible?

A

Yes

55
Q

What is the chemical equation for ADP being converted into ATP?

A

ADP + Pi + free energy -> ATP + H2O

56
Q

What is the change in Gibbs free energy for hydrolysis of one ATP under standard conditions?

A

-7.3 kcal/mole or -30.5 kJ/mole

57
Q

What is the change in Gibbs free energy for hydrolysis of one ATP under cellular conditions?

A

-14 kcal/mole or -57 kJ/mole

58
Q

How stable is ATP?

A

It is highly unstable and will spontaneously dissociate into ADP and Pi if not used

59
Q

In what form is energy released when ATP dissociates spontaneously?

A

It is released as heat energy

60
Q

energy coupling

A

when the energy from an exergonic reaction is used to drive another reaction

61
Q

phosphorylation

A

when a phosphate group binds to another molecule

62
Q

Do enzymes alter the free energy of a reaction?

A

No, they only change the activation energy required to start the reaction

63
Q

substrate

A

the reactants that bind to an enzyme

64
Q

active site

A

the location where the substrate binds with the enzyme

65
Q

How specific are enzymes for each substrate?

A

They is generally a unique enzyme for each substrate

66
Q

Why are enzymes so specialised?

A

Due to the complexity of enzymes as most of them are intricately composed and folded proteins

67
Q

What can happen to an enzyme if conditions are too extreme?

A

The enzymes can denature and lose its properties as an enzyme

68
Q

Which model previously describes how an enzyme binds to its substrate?

A

The “lock-and-key” model

69
Q

induced fit

A

model that describes how an enzyme binds to its substrate

70
Q

What does the induced fit model describe?

A

As the enzyme and substrate come together, the enzyme conforms to fit the substrates shape

71
Q

enzyme-substrate complex

A

when an enzyme binds to its substrate

72
Q

How does an enzyme promote chemical reactions through orientation?

A

Enzymes bring reactant substrates together in an optimal orientation for reacting

73
Q

How does an enzyme promote chemical reactions through environment?

A

The particular arrangement of certain amino acids can create an ideal environment for a reaction to occur

74
Q

How does an enzyme promote chemical reactions by altering the substrate directly?

A

It can contort the substrate to reach its transition state

75
Q

How does an enzyme promote chemical reactions by getting directly involved in the reaction?

A

It can provide the necessary substances for the chemical reaction to occur

76
Q

What ways can an enzyme promote chemical reactions?

A
  1. Orient substrates in an ideal position for reacting
  2. Create an ideal reacting environment
  3. By contorting the substrates into their transition state
  4. By taking part in the reaction itself
77
Q

Does an enzyme change after a chemical reaction?

A

No, it always reverts to its original form

78
Q

competitive inhibition

A

inhibitor molecules bind to the active sites of enzymes to prevent substrates from binding instead

79
Q

noncompetitive inhibition

A

inhibitor molecules bind to the enzyme in places other than the active and allosteric site and still prevents the substrate from binding to the active site

80
Q

How does competitive inhibition affect rate of reaction?

A

It slows the initial rate but does not affect the maximal rate

81
Q

How does noncompetitive inhibition affect rate of reaction?

A

It slows the initial rate and lowers the maximal rate

82
Q

allosteric site

A

site at which the inhibitor molecule binds to during allosteric inhibition

83
Q

allosteric inhibition

A

inhibitor molecule binds to a site other than the active site which conforms the active site to decrease affinity for the substrate

84
Q

allosteric activation

A

activator binds to allosteric site which conforms the active to increase affinity for the substrate

85
Q

How many polypeptide chains comprise most allosterically regulated enzymes?

A

More than one polypeptide

86
Q

What are the two types of enzyme helper molecules?

A

Cofactors and coenzymes

87
Q

cofactor

A

inorganic ions that act as enzyme helper molecules

88
Q

What cofactor does DNA polymerase need to function?

A

Zn++

89
Q

coenzyme

A

organic molecules that act as enzyme helpers

90
Q

What is the most common source of coenzymes?

A

Dietary vitamins

91
Q

How can enzymes be further regulated in cells?

A

They can be compartmentalised into cell organelles

92
Q

feedback inhibition

A

using an enzyme’s reaction products to regulate its own production

Biology (9 decks)

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