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.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

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

A

Draw a tangent at time of 0.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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.
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

What is the activation energy?

A

The MINIMUM energy required to INITIATE a chemical reaction.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What is a transition state?

A

The HIGHEST energy point in the reaction.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

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

A

Highest number of molecules with a particular energy.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

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

A

Number of Molecules

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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.
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

The rate of reaction depends on what?

A

Concentration of Reactants.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

What is the general form of the rate law?

A

Rate= k [A]m [B]n

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

How do you find the order of a reaction?

A

Add the reaction order of each reagent together.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

What does half life depend on?

A

RATE CONSTANT NOT on CONCENTRATION of reactant

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

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

A

First Order Reactions.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

What is the rate determining step?

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
What does the rate equation include?
Molecules INVOLVED in the rate determining step.
26
What is Molecularity?
The number of INDIVIDUAL molecules of the reacting species taking part in the rate determining step of a reaction
27
Kinetically- what reaction conditions are favourable?
A FAST reaction with a LOW activation energy.
28
Thermodynamically- what reaction conditions are favourable?
A reaction which leaves the system in a MORE stable state is favourable
29
How does a catalyst reduce the activation energy of a reaction?
By bringing reactants CLOSER together. | WEAKEN bonds in reactants STABLISING the transition state.
30
What is an enzyme?
Biological Catalyst
31
What type of protein is an enzyme mainly?
Globular Proteins.
32
Why are enzymes specific?
Only catalyse one reaction.
33
Enzymes- What do Oxidoreductatses do?
Transfer electrons/ hydrogens from one molecule to another.
34
Enzymes- What do Transferases do?
Transfer one functional group to another.
35
Enzymes- What do Hydrolyses do?
Catalyse hydrolysis reactions.
36
Enzymes- What do Lyases do?
Breaking of chemical bonds in elimination reactions.
37
Enzymes- What do Isomerases do?
Structural changes in a molecule.
38
Enzymes- What do Ligases do?
Joining of two substrates.
39
What is the lock and key Model?
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
What is the induced fit model?
Active site of the enzyme slightly CHANGES shape so the substrate is complementary to the enzyme’s active site.
41
What factors influence enzyme activity?
NON SPECIFIC- Temperature & pH. KINETICS- Concentration. SPECIFIC- Cofactors & Coenzymes & Inhibitors.
42
What happens to a reaction when the temperature of the reaction is above 37oC?
Enzyme denatures.
43
What is PCR?
Extremophile bacteria can be used to amply DNA and detect molecules.
44
How does pH effect an enzyme?
PROTONATION of ENZYME’S ACTIVE SITE. PROTONATION of SUBSTRATE. CONFORMATION of ENZYME. STABILITY of ENYME.
45
What is Vmax? What does Vmax indicate?
Limiting velocity an enzyme can get to, which indicates how good the enzyme is at catalysing a reaction by turning substrate to product.
46
What is Km?
Km is HALF of VMAX and is how efficient the enzyme is at binding to substrate.
47
What does a small Km for a reaction show?
Efficiently catalyses a reaction at low concentrations of substrate.
48
What does a large Km for a reaction show?
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
When does an aponenzyme become activated?
By the binding of coenzyme or cofactor to enzyme.
50
What is a Holoenzyme?
Holoenzyme is formed when associated cofactor or coenzyme binds to the enzyme's active site.
51
What is a competitive inhibitor?
Inhibitor binds to FREE ENZYME only, usually in the active site.
52
What is an irreversible inhibitor? How does it modify the structure?
These inhibitors bind using COVALENT bonds cannot be removed. Modify the structure or removes the activity of the active site.
53
What is an allosteric inhibitor?
Inhibitor does not bind to active site- binds to regulatory site.
54
Name some examples of irreversible inhibitors?
Aspirin Organophosphates Suicide inhibitors
55
What is an non- competitive inhibitor?
Inhibitors bind to free enzyme and enzyme-substrate complex EQUALLY.
56
What is an uncompetitive inhibitor?
Inhibitor binds to ENZYME-SUBSTRATE COMPLEX.
57
What happens to Km and Vmax of a competitive inhibitor? Why?
Change in Km No change Vmax Inhibitor prevents substrate binding by blocking binding site.
58
What happens to Km and Vmax of a non- competitive inhibitor?
No change to Km | Change to Vmax
59
What happens to Km and Vmax of a uncompetitive inhibitor?
Change to Km | Change to Vmax
60
If the enzyme and inhibitor have a higher affinity the mixed inhibitor will be similar to which other inhibitor?
Competitive Inhibitor.
61
If there is a higher affinity for enzyme substrate complex with inhibitor, then mixed inhibitor will be similar to which other inhibitor?
Uncompetitive inhibitor.