2. Energetics and Enzymes Flashcards

1
Q

1st Law of Thermodynamics

A

Energy can neither be created nor destroyed

Simply converted from one form to another

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2
Q

2nd Law of Thermodynamics

A

In any isolated system the degree of disorder can only increase.

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3
Q

Entropy

A

Amount of disorder in a system

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4
Q

Reactions proceed spontaneously towards

A

products with greater entropy

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5
Q

Gibb’s Free energy

A

amount of energy within a molecule that could perform useful work at a constant temperature.
Denoted by G with units kJ/mole§

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6
Q

Delta G

A

measures amount of disorder that results from a particular reaction

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7
Q

Calculate delta G

A

Free energy (Products) - Free energy (Reactants)

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8
Q

A reaction can only proceed spontaneously if

A

Delta G is negative

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9
Q

Pathways in cells that synthesise molecules are generally energetically unfavourable, how do they still occur?

A

Take place because they are coupled to an energetically favourable one.
Providing sum of delta G for overall reaction is still negative, reaction will proceed.

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10
Q

What do the majority of energetically unfavourable biochemical reactions rely on?

A

Hydrolysis of high-energy phosphate bonds e.g. those in ATP.

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11
Q

Phosphoanhydride bonds have a large negative delta G of hydrolysis

A

= High energy bonds

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12
Q

Delta G when converting ATP to ADP + Pi

A

-31 kJ/mol

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13
Q

In a biological setting, some energetically favourable reactions won’t occur at a rate useful for life

A

Unless catalysed by enzymes

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14
Q

Why is combustion of glucose energetically favourable?

A

It has a highly negative delta G

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15
Q

Why does glucose not spontaneously combust?

A

Because it has activation energy

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16
Q

Activation energy

A

Minimum energy required for a reaction to occur

17
Q

How can activation energy be overcome?

A

Enzymes provide an alternative reaction pathway

Lowering activation energy required

18
Q

Enzyme

A

A protein that acts a as a catalyst to induce chemical changes in other substances
Itself remaining apparently unchanged by the process

19
Q

What effect do enzymes have on rate of reaction?

A

Drastically increase rate of reaction

Lower energy barriers impeding chemical reactions

20
Q

Enzyme shape

A

Extremely specific due to their conformation

21
Q

What do enzymes do to their substrate?

A

Bend their substrates in such a way that bonds to be broken are stressed
Substrate molecule resembles transition state

22
Q

Transition state

A

Particular conformation of substrate in which atoms of the molecule are rearranged geometrically and electronically so the reaction can proceed
Makes them more amenable to reaction with other molecules

23
Q

How do enzymes work?

A

Substrate molecule binds tightly to enzyme active site
Arrange substrate in such a way that bonds are strained.
Key residues within enzyme participate in either the making or breaking of bonds by altering arrangement of electrons within substrate in the form of oxidation (-electrons from molecule) or reduction reactions (+ electrons).

24
Q

When enzymes cause oxidation/ reduction, as cellular environment is generally aqueous

A

Substrate molecule gains an electron & simultaneously gains a proton

25
Lock and Key model
Shape of substrate (key) matches active site (lock) of enzyme. Explains specificity of most enzymes for a single substrate.
26
Induced fit model
Substrate induces a change in conformation of the enzyme which results in formation of the active site. Upon release of products, enzyme reverts back to its original conformation
27
What is an enzyme found in nasal secretions and tears?
Lysozyme
28
What does lysozyme do?
Catalyses hydrolysis of sugar molecules in bacterial cell wall necessary for their structure. With this bond broken, bacteria lyse & die. 1st line of defence against bacteria
29
What does lysozyme hydrolyse?
Alternating polysaccharide copolymers of N-acetyl glucosamine (NAG) and N-acetyl muramic acid (NAM) which represent the "unit" polysaccharide structure of many bacterial cell walls.
30
Where does lysozyme cleave?
At Beta(1-4) glycosidic linkage, connecting C1 carbon of NAM to C4 carbon of NAG.
31
Which acidic residues are essential for catalysis by lysozyme?
Glu-35 and Asp-52
32
Mechanism of action for lysozyme
1. Glu-35 protonates Oxygen in glycosidic link between the 2 sugars- breaking glycosidic bond. 2. A water molecule enters & is deprotonated by Glu-35. 3. Asp-52 stabilises the positive charge in the transition state. 4. Hydroxide ion attacks remaining sugar molecule adding an OH group to it. 5. Proton is transferred to Glu-35 to return it to it's original state. 6. Glu-35 & Asp-52 are both in their original state to continue catalysis.
33
Chemical reactions speed up as temperature is increased
Catalysis increases at higher temperatures
34
Each enzyme has a temperature and pH optimum
beyond which its conformation is denatured | Enzyme becomes inactive
35
Coenzyme
an organic non-protein compound that binds with an enzyme to catalyse a reaction
36
Example of a coenzyme: | NAD+ (Nicotinamide adenine dinucleotide)
No effect on its own but functions only after binding to a protein. Vital component of many dehydrogenation reactions
37
How does NAD+ catalyse dehydrogenation of substrates?
By readily accepting a hydrogen atom & 2 electrons