Metabolism and Biogenergetics. Flashcards

1
Q

What does Metabolism do?

A

It allows all living things to grow, reproduce and move etc.
It enables cells to transform energy, from light, food etc.
To use Chemical energy; the synthesis of macromolecules and perform biological ‘work’

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2
Q

How are organisms classified?

A

From their source of energy and their source of carbon for the synthesis of cellular material - chemotroph (transform chemical energy) phototroph - need some preformed organic nutrients.
Heterotroph and autotrophs.

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3
Q

How many metric tons of carbon are cycling through the biosphere?

A

4 x 10^11 metric tons of carbon.

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4
Q

What is a metabolome?

A

This is a term for all metabolites in a cell or system

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5
Q

What is metabolomics?

A

These are the systemic characteristics of metabolome including under specific conditions.

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6
Q

What are catabolic pathways? What do they do?

A

These are convergent pathways which transform fuels into cellular energy ex: ATP, NADH, NADPH and FADH.

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7
Q

What are anabolic pathways? What do they do?

A

These are divergent and require cell energy to synthesis diverse macromolecules from small precursor molecules.

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8
Q

How regulated in metabolism? How integrated is it?

A

It is highly regulated and is integrated into the systems.

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9
Q

Which receptor enhances the sars cov -2 entry?

A

HDL receptor.

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10
Q

What is bioenergetics?

A

This is the quantitative study of energy transductions in living cells/organisms/systems.
The amount of free energy available to do work = free energy G
If reaction at equilibrium = 0
If reaction occurs spontaneously if delta G negative = EXERGONIC

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11
Q

What drives biochemical reactions?

A

Enzymes - makes them more thermodynamically favourable and specific. Enzymes allow for this.

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12
Q

What are the 2 laws of thermodynamics?

A

Total amount of energy in universe is constant.

Universe tends towards disorder entropy, X of universe increases.

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13
Q

What is thermodynamics referred as/measured in?

A

The change in Gibbs free energy, the delta - occurs in cell not a free chem reaction.

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14
Q

What are the different terms of reactions from occurring spontaneously (neg) and not occurring spontaneously (pos)?

A

Exergonic (neg)

Endergonic (pos)

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15
Q

What can a a thermodynamically favorable reaction in metabolism be driven by?

A

By a thermodynamically favourable one.

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16
Q

Standard free energy change is?

A

Additive

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17
Q

What enzyme allows for glycolysis?

A

Hexokinase.

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18
Q

Glycolysis generic formula:

A

C6H12O6

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19
Q

What does loss of ATP lead to ?

A

Cell injury/cell death.

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20
Q

What charge do the phosphate groups have in ATP?

A

Negative, they repel eachother.

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21
Q

What is the bond between the triphosphate in ATP?

A

Phosphoanhydride bond, the breaking of this bond creates/transfers energy. Usually exergonic. Each of these bonds/break/hydrolysis has a high negative free energy change.

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22
Q

Where is ATP synthesised?

A

In the mitochondria, inner foldings. Symbiotic bacteria descendent.

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23
Q

What is the synthesis of ATP called?

A

Oxidative phosphorylation.

24
Q

What are other examples of other phosphorylated compounds besides ATP?

A

Phosphoenolpyruvate and phosphocreatine (supplement - muscle) and some non-phosphorylated compounds ex: thioesters.
These all have large free energies of hydrolysis and can drive metabolic processes.

25
Q

How much energy is released by ATP hydrolysis?

A

-30.5kJ/mol

26
Q

How much energy is released by complete oxidation of glucose and palmitate?

A

Glucose: -2840 kj/mol
Palmitate: -9770 kj/mol

27
Q

What do kinases use for cell signalling?

A

ATP

28
Q

What does OIL RIG stand for?

A

Oxidation is loss, reduction is gain.

29
Q

What is the basis of catabolism?

A

Oxidation - loss of electrons/giving.

30
Q

What is the basis of anabolism?

A

Reduction - using/taking of electrons

31
Q

What is a reducing equivalent?

A

This is a single electron equivalent participating in redox reactions.

32
Q

What are reduction potentials?

A

This is a measure of the affinity for electrons.

33
Q

What form are electrons removed from living cells most often in catabolism?

A

Hydrogen.

34
Q

What is the most electronegative (hog electrons) element in living cells?

A

Oxygen - pulls electrons

35
Q

What does electron motor force provide energy to?

A

To a variety of molecular energy transducers - ATP synthase, ATP and other enzymes allowing systems to work in the cell.

36
Q

What is an example of redox in the body?

A

Hydrogen and fluorine.

37
Q

What does biological oxidation in catabolism often involve?

A

The removal of hydrogen atoms

38
Q

What synthesises ATP?

A

The electron transport chain.

39
Q

What enzymes are used in the removal of hydrogen atoms? Which cofactors?

A

Dehydrogenases (enabling carbon hydrogen atoms to break down), NAD, FAD

40
Q

What enzymes are used in anabolism ? The addition of hydrogen atoms?

A

Hydrogenases.

41
Q

What are the 4 major electron carriers in metabolism?

A

NAD, FAD, NADP, FMN - metabolism relies heavily on these biomolecules and are specifically designed to be great electron carrier molecules by harvesting and collecting electron energy.

42
Q

What is usually covalently attached to FAD?

A

Enzymes

43
Q

What does NAD generally function system wise?

A

Catabolism

44
Q

How does NADP function?

A

Through anabolism.

45
Q

What do NAD and NADP derive from vitamin wise?

A

Niacin, vitamin B3 (precursor NAD, NADP)

46
Q

What is a dietary deficiency of niacin called?

A

Pellagra - skin, gut and brain problems.

47
Q

What is the precursor of FAD?

A

Riboflavin

48
Q

Is the more NAD or NADP in cells?

A

NADP.

49
Q

What part of the NADP/NAD accepts a hydride ion?

A

The nicotinamide ring. - 2 electrons and one proton.

50
Q

Where can alcohol dehydrogenase be found?

A

In the stomach and the liver - allows for the consumption of alcoholic beverages a natural function to oxidise/catabolise alcohols by bacteria in the gut.

51
Q

What does FAD stand for?

A

Flavin Adenine dinucleotide

52
Q

What does FMN stand for?

A

Flavin Mononucleotide.

53
Q

What are FAD and FMN derived from ?

A

Riboflavin Vitamin B2 - Milk, cheese.

54
Q

How are FAD and FMN bound to dehydrogenases and what are these called?

A

Covalently , called flavoproteins.

55
Q

What is the ring structure in FMN/FAD called and what does it do?

A

Isoalloxazine ring - accepts 1 or 2 electrons. Fused ring structure accepts one or two electrons in the form of hydrogen atoms,

56
Q

What is EMF?

A

This is the energy per unit electric charge that is imparted by an energy source.

57
Q

What is the difference between FAD and FMN?

A

One is a mononucleotide and the other is a dinucleotide.