Bioenergetics Flashcards

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1
Q

What are the energy transformations in cells?

A

Light to chemical, chemical to chemical (carbon as a source of ATP), chemical to mechanical

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2
Q

What is the first law of thermodynamics?

A

Energy can neither be created nor destroyed.

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3
Q

What is the second law of thermodynamics?

A

All events in the universe tend to proceed downhill from a state of high energy to low energy. There is a tenancy for disorder to increase with each energy change.

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4
Q

What is the Gibbs Free Energy equation?

A

DeltaH = DeltaG + TDeltaS
OR
DeltaG = DeltaH - TDeltaS

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5
Q

What is DeltaH?

A

the potential energy (enthalpy) (PE in bonds)

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6
Q

What is DeltaG?

A

the free energy (work energy)

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7
Q

What is DeltaS?

A

Energy lost to disorder (entropy)

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8
Q

For an endergonic reaction, DeltaG will be _____ and the reaction will occur _____.

A

Greater than zero, non-spontaneous

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9
Q

For an exergonic reaction, DeltaG will be _____ and the reaction will occur ______.

A

Less than zero, spontaneously

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10
Q

Generally, DeltaG is spontaneous when DeltaH is _____ and DeltaS is ______.

A

Less than zero, greater than zero.

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11
Q

DeltaG can negative if DeltaH is ______ or ______, and DeltaS is _______ or ______.

A

Much less that zero, about zero, about zero, much greater than zero.

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12
Q

Enthalpy is the potential bond energy minus the ________.

A

Energy released when broken/energy needed to form

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13
Q

What is DeltaG^0

A

The spontaneity of a reaction under standard conditions (298K, 1M concentration of reactants and products.

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14
Q

How do you calculate DeltaG from DeltaG^0

A

DeltaG = DeltaG^0 + 2.303 R T log ([C][D])/([A][B]). Cells can only manipulate the concentration portion of this equation

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15
Q

What are the mechanisms used to force cells to undergo endergonic reactions?

A
  1. Altering ratio of product to reactants (products can be kept low by servind as reactants in following rxns) and 2. Coupling rxn with exergonic rxn.
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16
Q

What exergonic reaction are endergonic reactions most frequently coupled to?

A

ATP hydrolysis

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17
Q

Enzymes change the _____, but not the ________ of a reaction.

A

Speed, thermodynamics

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18
Q

What does the rate of reaction depend on?

A

Number of reactants with sufficient KE to overcome activation energy barrier.

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19
Q

How do enzymes change to rate of reactions?

A

They lower the activation energy barrier.

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20
Q

What are the three ways enzymes can change rate of reaction?

A
  1. Changing substrate orientation (bringing substrates together in correct orientation), 2. Changing the substrate reactivity (substrate influenced by side chains at active site that alter chem. properties), 3. inducing physical strain in substrate (changing conformation)
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21
Q

With regards to measuring enzyme activity, what is the Vmax?

A

The maximum speed of an enzyme-catalyzed reaction

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22
Q

With regards to measuring enzyme activity, what is the Km?

A

Substrate concentration needed to operate liniarly.

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23
Q

With regards to measuring enzyme activity, what how are Vmax and Km related?

A

The Km is the x-value at 1/2 the Vmax

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24
Q

With regards to measuring enzyme activity, what is on the x-axis. The y-axis?

A

Substrate concentration, initial reaction velocity

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25
Q

What is the Michaelis-Menten Equation?

A

V=Vmax * ([S])/([S] + Km)

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26
Q

What is the Lineweaver-Burk equation?

A

1/Vinit’l = (Km/Vmax) * (1/[S]) + 1/Vmax

27
Q

What is the slope of a Lineweaver-Burk plot?

A

Km/Vmax

28
Q

What is the y-int of a Lineweaver-Burk plot?

A

1/Vmax

29
Q

What is the x-int of a Lineweaver-Burk plot?

A

-1/Km

30
Q

Why is the Lineweaver-Burk plot often preferred?

A

For the Michaelis-Menten plot, it is hard to tell exactly when you have reached the Vmax. The Lineweaver-Burk plot eliminates this uncertainty.

31
Q

What enzyme does Aspirin inhibit?

A

COX-1 (produces signalling molecules that induce pain and inflammation)

32
Q

What are competitive inhibitors?

A

Affect Km not Vmax, they compete with substrate for active site and can be overcome by adding more substrate

33
Q

What are non-competitive inhibitors?

A

Affect Vmax not Km, act at different site on the enzyme and cannon be overcome by increasing substrate.

34
Q

Non-competitive inhibitors________ Vmax.

A

Reduce

35
Q

Competitive inhibitors _______ Km.

A

Increase

36
Q

Anabolism is an _____ reaction, meaning DeltaS is _____.

A

Endergonic, negative

37
Q

Catabolism is an _______ reaction, meaning DeltaS is _______.

A

Exergonic, positive

38
Q

What atom are the electrons stripped from in catabolism?

A

Carbon

39
Q

The ETS generates a _________ that drives ATP synthase.

A

H+ gradient

40
Q

Where does glucose lie on the scale of how easily electrons can be extracted from it (what hydrocarbon does it mirror)?

A

It is on the higher energy side od=f the spectrum like methanol. This means carbon is more electronegative than hydrogen and the electrons can be more readily extracted.

41
Q

Why is ATP such an effective storage molecule?

A

The phosphate transfer potential of ATP is mid-scale, meaning it can be either a donor or acceptor for spontaneous reactions.

42
Q

Where does aerobic respiration begin?

A

In the cytoplasm

43
Q

What is the first step in catabolism?

A

Glycolysis

44
Q

What are the reagents for glycolysis?

A

Glucose, 2 ADP, 2 Pi, NAD+

45
Q

What are the products of glycolysis?

A

2 Pyruvate, 2 ATP, 2 NADH

46
Q

How does glycolysis force DeltaG to be less that 0?

A

It couples with ATP hydrolysis

47
Q

Where does the TCA cycle occur?

A

In the mitochondrial matrix space

48
Q

How many cycles of the TCA cycle does it take to oxidize one glucose?

A

2

49
Q

What are the reagents for the TCA cycle?

A

2 ATP, 2 Pyruvate, 2 NADH

50
Q

What are the products of the TCA cycle?

A

4 NADH+ and 1 FADH2

51
Q

What is used to drive ATP synthase in the mitochondria?

A

H+ gradient accross inner mitochondrial membrane

52
Q

How is the H+ gradient made for ATP synthase?

A
  1. Transfer high energy e- from glucose to NADH/FADH2 2) Transfer high energy e- from NADH/FADH2 to electron carriers 3) Energy is released from the electron transport to pump H+ from matrix to IMS 4) Flow of H+ back through ATP synthase powers activity
53
Q

What is REDOX potential? (Enot)

A

The tendency to accept or donate electrons

54
Q

What does a high REDOX potential mean?

A

High tendency to accept electrons, low tendency to donate

55
Q

What does a low REDOX potential mean?

A

Low tendency to accept electrons, high tendency to donate

56
Q

What is the rule of thumb when using the table of standard REDOX potentials?

A

Electron flow is always downward

57
Q

What is the equation for calculating REDOX potential?

A

DeltaG(not) = -nF(DeltaE of acceptor - donor)

58
Q

What order to electrons travel through the complexes in?

A

Complex 1 –> complex III –> complex IV

59
Q

What is the ATP yield when e- transfer is initiated by NADH (in ETC)

A

3 ATP

60
Q

What is the ATP yield when e- transfer is initiated by FADH2? (in ETC)

A

2 ATP

61
Q

What order does NADH go through the ETC? What are the carriers?

A

Enters at complex I, ubiquinome carries to complex III, cytochrome C carries to complex IV

62
Q

What order does FADH2 go through the ETC? What are the carriers?

A

Enters at complex II, ubiquinome transports to complex III, cytochrome C transports to complex IV

63
Q

What is the final electron acceptor of the ETC?

A

oxygen

64
Q

How many electrons are transported at a time in the electron transport chain?

A

one–free radicals are dangerous