MODULE 11: Chapter 11.2 Flashcards

1
Q

Where do glycolysis and the citrate cycle take place?

A

Glycolysis takes place in the cytosol, while the citrate cycle occurs in the mitochondrial matrix.

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2
Q

What initiates the electron transport system?

A

The oxidation of NADH by the mitochondrial electron transport system, starting with complex I.

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3
Q

How many discrete electron carriers are involved in the electron transport system?

A

As many as 20 discrete electron carriers.

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4
Q

What is the end product of the electron transport system?

A

The reduction of molecular oxygen to form water.

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5
Q

What is the primary function of coenzyme Q in the electron transport system?

A

Coenzyme Q serves as a mobile electron carrier that transports electrons laterally in the membrane.

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6
Q

What happens to ATP synthesis if electron transfer in the electron transport system is inhibited?

A

There is a loss of ATP synthesis by the ATP synthase complex.

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7
Q

Name one inhibitor of the electron transport system.

A

Rotenone, hydrogen cyanide, carbon monoxide, or antimycin A.

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8
Q

What are the four functional components of the electron transport system?

A
  1. Three large multi-subunit protein complexes (I, III, IV)
  2. Coenzyme Q (ubiquinone)
  3. Three membrane-associated FAD-containing enzymes
  4. Cytochrome c.
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9
Q

What is the biochemical standard reduction potential (E°′) for NAD⁺/NADH?

A

-0.32 V.

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10
Q

How do reduction potentials change throughout the electron transport system?

A

Reduction potentials generally increase with each reaction in the electron transport system.

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11
Q

What is the role of cytochrome c in the electron transport system?

A

Cytochrome c carries electrons one at a time from complex III to complex IV.

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12
Q

What is the mass and number of subunits for complex I?

A

Complex I has a mass of 850 kDa and contains 42 subunits.

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13
Q

What prosthetic groups are associated with complex II?

A

FAD and Fe–S.

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14
Q

What are the two mechanisms proposed for proton translocation across the membrane?

A
  1. A redox loop mechanism
  2. A redox-driven proton pump.
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15
Q

How does complex I contribute to proton translocation?

A

Complex I translocates 4 H⁺ from the matrix side to the intermembrane space.

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16
Q

What is the structure of complex I from mammals based on cryo-electron microscopy?

A

It is shaped like a sideways ‘L’ and contains more than 40 transmembrane α helices.

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17
Q

What happens to the Fe–S centers during electron transfer in complex I?

A

They carry one electron at a time from one end of the complex to the other.

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18
Q

What is the reduction potential of O2/H2O?

A

+0.82 V.

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19
Q

What is the result of the oxidation of NADH in complex I?

A

The reduction of coenzyme Q to form QH2 (ubiquinol) and the translocation of protons.

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20
Q

Fill in the blank: Complex II is also known as _______.

A

succinate dehydrogenase.

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21
Q

True or False: Complex IV is the least abundant complex in the electron transport system.

A

False.

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22
Q

What is the main role of FMN in complex I?

A

FMN accepts two electrons from NADH.

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23
Q

What is the total number of protons translocated when electrons are derived from FADH2?

A

6 H⁺.

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24
Q

What does the Q cycle in complex III utilize?

A

A redox loop mechanism for proton translocation.

25
What is the function of the iron-sulfur (Fe–S) centers in complex I?
They facilitate electron transfer through redox reactions.
26
What is the effect of rotenone on complex I?
It blocks electron transfer by preventing a redox reaction between two Fe–S centers.
27
What is the equation for the reaction involving NADH and coenzyme Q?
NADH + Q + 5 H⁺ → NAD⁺ + QH₂ + 4 H⁺ ## Footnote This equation represents the transfer of electrons from NADH to coenzyme Q.
28
What are the three critical roles of coenzyme Q in the electron transport system?
* Mobile electron carrier transporting electrons between complexes I, II, and III * Entry point for electron pairs from citrate cycle, fatty acid oxidation, and glycerol-3-phosphate dehydrogenase * Converts 2 e− transport system into 1 e− transport system in complex III via the Q cycle
29
What is the hydrophobic tail of coenzyme Q made of?
Repeating isoprenoid units ## Footnote In humans, the hydrophobic tail consists of 10 isoprenoid units, totaling 50 carbons.
30
What is the common name for coenzyme Q with a hydrophobic tail of 10 isoprenoid units?
Coenzyme Q10 or CoQ10 ## Footnote CoQ10 is sold as an over-the-counter nutritional supplement.
31
What is the function of succinate dehydrogenase in complex II?
Catalyzes the oxidation of succinate to fumarate and transfers electrons to FAD ## Footnote It participates in both the electron transport chain and the citrate cycle.
32
What is the net reaction of succinate oxidation by succinate dehydrogenase?
Succinate + FAD → Fumarate + FADH₂ ## Footnote The electron pair from succinate is transferred to FAD.
33
What components are found in mammalian succinate dehydrogenase?
* Three iron–sulfur centers (two 4 Fe–4 S and one 2 Fe–2 S) * A b-type heme (cytochrome b560)
34
What is the function of complex III in the electron transport chain?
Transfers electrons from QH₂ to cytochrome c one at a time ## Footnote Complex III has multiple protein subunits and serves as a docking site for QH₂.
35
What are the two binding sites for ubiquinone in complex III called?
QP and QN ## Footnote QP is closer to the intermembrane space and QN is closer to the mitochondrial matrix.
36
What is the overall reaction of QH₂ oxidation by complex III?
QH₂ + 2 H⁺ → Q + 4 H⁺ + 2 reduced cytochrome c ## Footnote This reaction translocates protons across the membrane.
37
What is cytochrome c?
A small protein (∼13 kDa) that transports one electron from complex III to complex IV ## Footnote It contains a heme group that binds iron.
38
What distinguishes oxidized and reduced cytochrome c?
Oxidized cytochrome c contains ferric iron (Fe³⁺) and reduced cytochrome c contains ferrous iron (Fe²⁺)
39
What types of cytochromes are there, and how are they classified?
* Type a * Type b * Type c ## Footnote They are classified based on the type of heme group they contain.
40
What is the absorption spectrum of reduced cytochrome c?
Shows peaks at 418 nm (γ), 534 nm (β), and 554 nm (α) ## Footnote Different cytochromes have distinct absorption spectra.
41
What is the function of complex IV in the electron transport chain?
Accepts electrons from cytochrome c and donates them to oxygen to form water ## Footnote This process translocates protons across the membrane.
42
What components are found in mitochondrial complex IV?
* Two copper centers (CuA and CuB) * Two heme groups (one in cytochrome a and one in cytochrome a3)
43
How does cytochrome c interact with complex IV?
Binds near CuA, which accepts electrons in a coupled redox reaction ## Footnote This interaction leads to the oxidation of cytochrome c.
44
What is the structure of the human complex IV protein?
It includes 14 subunits, two copper centers, and two hemes identified using high-resolution cryo-electron microscopy.
45
How many H⁺ are involved in the complex IV reactions?
A total of four H⁺ are involved: 2 H⁺ translocated into the intermembrane space and 2 H⁺ used to form H2O.
46
What is the function of cytochrome c in the electron transport system?
Cytochrome c transports only 1 e− at a time and must make two trips to transfer a pair of electrons from NADH or FADH2 to O2.
47
What is the difference in H⁺ translocation between complex I and complex II?
Complex I translocates 10 H⁺, while complex II translocates only 6 H⁺.
48
What is proton-motive force?
The contributions of ΔpH and Δψ to the stored energy in the electrochemical proton gradient.
49
What is the equation for calculating the change in biochemical standard free energy (ΔG°′)?
ΔG°′ = −nFΔE°′
50
What are the E°′ values for NAD⁺/NADH and O2/H2O?
NAD⁺/NADH is −0.32 V and O2/H2O is +0.82 V.
51
What is the ΔG°′ for translocation of 10 H⁺ across the membrane when NADH is oxidized?
ΔG°′ = −220.0 kJ/mol of NADH oxidized.
52
What is the ΔG value for the proton-motive force at 37 °C?
ΔG = −20.80 kJ/mol.
53
What is the efficiency of the electron transport system based on free energy calculations?
Approximately 94%.
54
What role does coenzyme Q play in the electron transport system?
Coenzyme Q is a mobile electron carrier that transports a pair of electrons (2 e−) in its reduced form of QH2.
55
What is the theoretical yield of ATP per NADH based on the change in free energy of −208 kJ/mol?
Theoretical yield is calculated using a value of ∼40 kJ/mol for ATP synthesis.
56
What is the actual yield of ATP per NADH?
Approximately 2.5 ATP/NADH.
57
What might account for the difference in efficiency based on free energy calculations and ATP yields?
Differences in energy conversion efficiencies in oxidative phosphorylation.
58
What are iron–sulfur (Fe–S) centers?
Electron carrier prosthetic groups found in complexes I, II, and III of the electron transport system.
59
Fill in the blank: The term _______ describes the potential energy of the proton concentration gradient plus the charge difference across the membrane.
proton-motive force