Lecture 3 + 4 Flashcards

1
Q

What is the rate of a reaction?

A

The CHANGE in CONCENTRATION of a species per unit of TIME.

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2
Q

From a graph how do you measure initial rate of reaction?

A

Draw a tangent at time of 0.

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3
Q

What 3 ideas does collision theory suggest?

A
  1. Reactions occur when particles COLLIDE, however not all collisions result in reactions.
  2. Particles must possess at least a MINIMUM amount of energy.
  3. Particles must approach each other in a certain RELATIVE ORIENTATION.
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4
Q

What factors affect rate of reaction?

A
  1. The OVERALL number of COLLISIONS occurring.

2. The NUMBER of particles with enough ENERGY to react.

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5
Q

What is the activation energy?

A

The MINIMUM energy required to INITIATE a chemical reaction.

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6
Q

What is a transition state?

A

The HIGHEST energy point in the reaction.

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7
Q

In a Maxwell- Boltzmen graph what does the peak show?

A

Highest number of molecules with a particular energy.

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8
Q

In a Maxwell- Boltzmen graph what does the area under the curve show?

A

Number of Molecules

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9
Q

When you increase the the temperature of a reaction, why does the rate of reaction increase? (2 Reasons)

A
  1. Particle speeds increases so collisions are more FREQUENT.
  2. Particles have MORE energy to overcome the energy barrier.
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10
Q

When a catalyst is added to a reaction, why does the rate of reaction increase?

A

Works by providing an ALTERNATIVE reaction PATHWAY with a LOWER activation energy so MORE particles now have the energy to react.

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11
Q

When increasing the surface of a solid reagent/ heterogenous catalyst, why does the rate of reaction increase?

A

Increases chances of a COLLISION because more particles are exposed.

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12
Q

When increasing the pressure of a gas, why does the rate of reaction increase?

A

Forces gas particles CLOSER together increasing the FREQUENCY of collisions so rate of reaction increases.

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13
Q

When increasing the concentration of a liquid, why does the rate of reaction usually increase?

A

LARGER number of particles so MORE collisions.

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14
Q

The rate of reaction depends on what?

A

Concentration of Reactants.

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15
Q

What is the general form of the rate law?

A

Rate= k [A]m [B]n

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16
Q

How do you find the order of a reaction?

A

Add the reaction order of each reagent together.

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17
Q

In a zero- order reaction the rate does not change, what does this mean?

A

The reaction depends on a catalytic Bottle- neck.

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18
Q

What is a CATALYTIC BOTTLE-NECK?

A

A CATALYTIC BOTTLE-NECK is where the reaction depends on a catalyse/ enzyme which has limited capacity. At working concentration with all active sites full, there is no effect when adding more substrate.

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19
Q

What is half life of a reaction?

A

The TIME taken for the CONCENTRATION of a reaction to drop to HALF of its original value

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20
Q

What does half life depend on?

A

RATE CONSTANT NOT on CONCENTRATION of reactant

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21
Q

Describe each line on a graph for ‘Rate vs Concentration’ for a Zero, First and Second Order reaction. Why are the lines shown like this?

A

Zero Order- Straight horizontal line. Rate not dependent on concentration of reactants.
First Order- Rate is proportional to concentration of a single reactant.
Second Order- The rate is proportional to the square of the concentration.

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22
Q

Which order of a reaction has a constant half- life?

A

First Order Reactions.

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23
Q

Describe each line on a graph for ‘Concentration vs Time’ for a Zero, First and Second Order reaction. What happens to half- life of each one?

A

Zero Order- A straight line showing a constant decline in concentration. Half life decreases as reaction progresses.
First Order- A slightly sloping curve which drops with a constant half life.
Second Order- The curve declines steeply at first then levels out. Half life increases as reaction progresses.

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24
Q

What is the rate determining step?

A

The overall rate of a multi- step reaction is governed by the SLOWEST step.

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25
Q

What does the rate equation include?

A

Molecules INVOLVED in the rate determining step.

26
Q

What is Molecularity?

A

The number of INDIVIDUAL molecules of the reacting species taking part in the rate determining step of a reaction

27
Q

Kinetically- what reaction conditions are favourable?

A

A FAST reaction with a LOW activation energy.

28
Q

Thermodynamically- what reaction conditions are favourable?

A

A reaction which leaves the system in a MORE stable state is favourable

29
Q

How does a catalyst reduce the activation energy of a reaction?

A

By bringing reactants CLOSER together.

WEAKEN bonds in reactants STABLISING the transition state.

30
Q

What is an enzyme?

A

Biological Catalyst

31
Q

What type of protein is an enzyme mainly?

A

Globular Proteins.

32
Q

Why are enzymes specific?

A

Only catalyse one reaction.

33
Q

Enzymes- What do Oxidoreductatses do?

A

Transfer electrons/ hydrogens from one molecule to another.

34
Q

Enzymes- What do Transferases do?

A

Transfer one functional group to another.

35
Q

Enzymes- What do Hydrolyses do?

A

Catalyse hydrolysis reactions.

36
Q

Enzymes- What do Lyases do?

A

Breaking of chemical bonds in elimination reactions.

37
Q

Enzymes- What do Isomerases do?

A

Structural changes in a molecule.

38
Q

Enzymes- What do Ligases do?

A

Joining of two substrates.

39
Q

What is the lock and key Model?

A

Only one SUBSTRATE (KEY) can fit into the enzyme’s ACTIVE SITE (LOCK) because both enzyme and substrate have a unique and fixed shape which is complementary to each other.

40
Q

What is the induced fit model?

A

Active site of the enzyme slightly CHANGES shape so the substrate is complementary to the enzyme’s active site.

41
Q

What factors influence enzyme activity?

A

NON SPECIFIC- Temperature & pH.
KINETICS- Concentration.
SPECIFIC- Cofactors & Coenzymes & Inhibitors.

42
Q

What happens to a reaction when the temperature of the reaction is above 37oC?

A

Enzyme denatures.

43
Q

What is PCR?

A

Extremophile bacteria can be used to amply DNA and detect molecules.

44
Q

How does pH effect an enzyme?

A

PROTONATION of ENZYME’S ACTIVE SITE.
PROTONATION of SUBSTRATE.
CONFORMATION of ENZYME.
STABILITY of ENYME.

45
Q

What is Vmax? What does Vmax indicate?

A

Limiting velocity an enzyme can get to, which indicates how good the enzyme is at catalysing a reaction by turning substrate to product.

46
Q

What is Km?

A

Km is HALF of VMAX and is how efficient the enzyme is at binding to substrate.

47
Q

What does a small Km for a reaction show?

A

Efficiently catalyses a reaction at low concentrations of substrate.

48
Q

What does a large Km for a reaction show?

A

LARGE Km means there is weak binding of enzyme to substrate so substrate will fit in to the active site but will not be changed to a product. Therefore little activity at low concentrations of substrate.

49
Q

When does an aponenzyme become activated?

A

By the binding of coenzyme or cofactor to enzyme.

50
Q

What is a Holoenzyme?

A

Holoenzyme is formed when associated cofactor or coenzyme binds to the enzyme’s active site.

51
Q

What is a competitive inhibitor?

A

Inhibitor binds to FREE ENZYME only, usually in the active site.

52
Q

What is an irreversible inhibitor? How does it modify the structure?

A

These inhibitors bind using COVALENT bonds cannot be removed.
Modify the structure or removes the activity of the active site.

53
Q

What is an allosteric inhibitor?

A

Inhibitor does not bind to active site- binds to regulatory site.

54
Q

Name some examples of irreversible inhibitors?

A

Aspirin
Organophosphates
Suicide inhibitors

55
Q

What is an non- competitive inhibitor?

A

Inhibitors bind to free enzyme and enzyme-substrate complex EQUALLY.

56
Q

What is an uncompetitive inhibitor?

A

Inhibitor binds to ENZYME-SUBSTRATE COMPLEX.

57
Q

What happens to Km and Vmax of a competitive inhibitor? Why?

A

Change in Km
No change Vmax
Inhibitor prevents substrate binding by blocking binding site.

58
Q

What happens to Km and Vmax of a non- competitive inhibitor?

A

No change to Km

Change to Vmax

59
Q

What happens to Km and Vmax of a uncompetitive inhibitor?

A

Change to Km

Change to Vmax

60
Q

If the enzyme and inhibitor have a higher affinity the mixed inhibitor will be similar to which other inhibitor?

A

Competitive Inhibitor.

61
Q

If there is a higher affinity for enzyme substrate complex with inhibitor, then mixed inhibitor will be similar to which other inhibitor?

A

Uncompetitive inhibitor.