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Biochemistry > Principles > Flashcards

Principles Flashcards

1
Q

How does glucose enter cells?

A

Via the sodium glucose symporters

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2
Q

What does hexokinase do to glucose?

A

Turns it to glucose 6-phosphate

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3
Q

What does phosphofructokinase do to fructo 6-phosphate?

A

Turns it to fructo 1,6-biphosphate

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4
Q

Pyruvate kinase is needed to make what?

A

Pyruvate

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5
Q

The three enzymes controlling irreversible pathways in glycolysis

A

Hexokinase, phosphofructokinase, pyruvate kinase

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6
Q

What is derived from niacin?

A

NAD+

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7
Q

What is regenerated through the metabolism of pyruvate?

A

NAD+

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8
Q

Where are the enzymes of the TCA cycle located?

A

The mitochondrial matrix, except succinate dehydrogenase which is located in the inner membrane

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9
Q

How many NADH + H+ and FADH2 produced in each turn of the TCA cycle?

A

3 NADH + H+ and 1 FADH2

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10
Q

What can pyruvate be converted to?

A

Alcohol, lactate, acetyl coA

alcohol dehydrogenase, lactate dehydrogenase

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11
Q

What catalyses the oxidative phosphorylation of pyruvate to acetyl coA?

A

Pyruvate dehydrogenase complex

3 enzymes involved, 2 extra for control and 5 cofactors

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12
Q

What is a major determination of glucose oxidation in well oxygenated tissues?

A

Pyruvate dehydrogenase complex (this reaction is irreversible lol)

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13
Q

How many high energy electrons in NADH+/FADH2?

A

2

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14
Q

How can the electron transfer potential be measured?

A

The redox potential/reduction potential of the compound

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15
Q

How can the phosphoryl transfer potential be measured?

A

The free energy change for the hydrolysis of ATP

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16
Q

What does a negative E’o mean?

A

Lower affinity for electrons than hydrogen

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17
Q

What is the standard free energy change proportional to?

A

The change in standard redox potential and the number of electrons transferred.

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18
Q

What is the change in standard redox potential and number of electrons transferred proportional to?

A

The change in free energy

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19
Q

How many of the 4 respiratory pumps, pump H+?

A

3

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20
Q

At which complex does FADH2 enter?

A

Complx 2 (this is part of the TCA cycle)

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21
Q

What do the respiratory chain proton pumps do?

A

Pump protons into the intermembrane space

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22
Q

How do protons flow back through from the intermembrane space to the inner matrix?

A

Through ATP synthase

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23
Q

The importance of the haem group in cytochrome?

A

Picks up and releases electrons

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24
Q

The glycerol-3-phosphate and malate shuttles are used to do what?

A

Transport NADH from the cytoplasm into the inner mitochondrial membrane

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25
Q

ATP yield from 1 glucose molecule?

A

30-32 molecules (depends on exact P/O ration and which shuttle was used)

26
Q

What is a hydrophobic interaction?

A

The interaction between a polar substance and a non-polar substance

27
Q

What is a van der Waals interaction?

A

Interaction of electrons between non-polar substances

28
Q

What is acylation?

A

Addition of an acyl group (RCO)

29
Q

Electrons are transferred from propane to oxygen to form what?

A

Water

30
Q

First law of thermodynamics?

A

Energy is neither created nor destroyed

31
Q

Second law of thermodynamics?

A

When energy is converted from one form to another, some of that energy becomes unavailable to do work

32
Q

What is a change in enthalpy?

A

A change in heat content H

33
Q

What is a change in entropy?

A

A change in order/randomness S

34
Q

What are exogernic reactions?

A

Reactions where the free energy of the products is greater than that of the reactants
These reactions can occur spontaneously

35
Q

Why is pH 7 included in standard conditions?

A

Because pH 0/ 1 mol H+ is extremely acidic for the human body

36
Q

^G values near 0 are characteristic of what?

A

Readily reversible reactions

Also remember, the closer a reaction is to equilibrium, the more free energy is released

37
Q

What does phosphoglucomutase do?

A

Catalyses the reaction of glucose 1-phosphate to glucose 2-phosphate and vice versa

38
Q

What do you do if the process is unfavourable?

A

Couple it to a favourable one (i.e one with a negative free energy change. A bit like hi-jacking) This is why ATP is used as a universal energy current

39
Q

Where will you find high energy anhydride bonds?

A

ATP

40
Q

Are reactions with ^G close to 0 used as control points?

A

No. Reactions with fairly large negative ^G values are used as control points. Flux through these points is controlled by altering the activity of the enzyme involved

41
Q

What does the acid dissociation (Ka) constant measure?

A

How readily an acid donates a proton

42
Q

Buffers and their pKa values?

A

When buffers are close to their pKa value, they tend to resist a change in pH upon small additions of acid/base

43
Q

What plots pH as a function of base to acid added?

A

A titration curve

44
Q

Zwitterions?

A

Lol a molecule without charged side groups i.e amino acids (these can be used as buffers)

45
Q

What is the isoelectric pH?

A

The pH at which an molecule has no net charge

46
Q

Why do amino acids have 2 pKa values?

A

Because they have 2 titratable groups

47
Q

Which angles can peptides rotate around?

A

The angle between the C and the carboxyl group

The angle between the C and the amino group

48
Q

What does proline do to alpha helices?

A

Breaks them

49
Q

What does the enzyme which carboxylates proline need?

A

Vitamin C

50
Q

What type of protein is collagen?

A

A fibrous protein

51
Q

Are globular proteins soluble in water?

A

Yes, most of their polar side chains are on the outside
Nearly all have masses of alpha helix and beta sheets
Fibrous proteins are not soluble in water

52
Q

What are involved in sulphide bond formation?

A

Cysteine molecules (SH)

53
Q

What contains repeating sequences of X, Y and Gly?

A

Tropocollagen

54
Q

Does collagen contain inta-chain H bonds?

A

No, only inter-chain H bonds

55
Q

In which condition does a mutation so that valine is produced instead of glutamic acid?
(single nucleotide sequence change)

A

Sickle cell anemia

valine interacts with other hydrophobic amino acids

56
Q

What are chaperone proteins?

A

Proteins which aid protein folding

57
Q

How do thiol agents (reducing agents) disrupt protein structure?

A

Reduce and therefore disrupt disulphide bonds

58
Q

ATP, citrate and H+ are negative modulators of what?

A

Phosphofructokinase

AMP and fructose 2,6-biphosphate are positive modulators

59
Q

Adenylate kinase?

A

2ADP->ATP + AMP

60
Q

What is the ‘energy charge’?

A

ATP/AMP ratio

61
Q

Succinate and FAD produce..?

A

Fumarate and FADH2

Biochemistry (4 decks)

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