Lecture 14: Energy Conversion in Mitochondria Flashcards

1
Q

Why is ATP production called chemiosmotic?

A

This process is called chemisomotic coupling since chemical bond formation (“chemi”) is linked to membrane transport processes (“osmotic”)

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2
Q

2 stages of ATP production?

A

Stage 1: – High energy electrons are used to set up a proton gradient across the mitochondrial inner membrane Stage 2: – ATP synthase (F-type ATPase) uses the proton gradient to drive ATP production

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3
Q

Outer membrane

A

– Permeable to small molecules

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4
Q

Inner membrane

A

– Cristea – Location of the respiratory chain (electron transport proteins) and ATP synthase

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5
Q

Matrix

A

• Tricarboxylic (TCA) acid cycle, aka Kreb cycle or citric acid cycle • Source of NADH (reduced NAD+, electron for ETS)

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6
Q

Food molecules can be broken down into what two things?

A

-fatty acids -pyruvate

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7
Q

Fatty acids and pyruvate are converted to _____ before entering the Krebs (TCA) cycle.

A

Acetyl-CoA

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8
Q

What protein is responsible for dividing mitochondria?

A

Dynamin

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9
Q

The ____ determines the position and timing of mitochondrial fission

A

ER

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10
Q

Mitochondria often align with ___

A

microtubules

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11
Q

Mitochondria are more prevalent in high energy tissues like….

A

cardiac muscle, sperm tails

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12
Q

___ is the primary donor of electrons for the ETS

A

NADH

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13
Q

FADH2 is also utilized as an electron donor, entering at ____

A

ubiquinone

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14
Q

NADH is generated by the catabolism of ___ to CO2 during the TCA cycle

A

acetyl-CoA

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15
Q

Acetyl-CoA is produced from glucose by ___

A

glycolosis

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16
Q

Acetyl-CoA is produced from fatty acids by ___

A

β-oxidation

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17
Q

NADH donates ___ electrons to the ETC

A

2

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18
Q

FADH2 donates ___ electrons to the ETC

A

4

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19
Q

The two components of the electrochemical proton gradient formed by the respiratory chain?

A

-Proton-motive force due to membrane potential (neg in matrix) -Proton motive force due to PH gradient (basic in matrix)

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20
Q

Proton translocating proteins contain…

A

“proton wires” which are rows of polar or ionic side chains or water molecules spaced at short distances so that proton can jump form one to the other

21
Q

Each subsequent participant in the electron transport chain has an increasingly ___ oxidation reduction (redox) potential

A

larger

22
Q

NADH readily donates its high energy electrons to ___ bound to proteins within the ETC.

A

metals

23
Q

Order of proteins in ETC?

A
24
Q

What are two types of electron carriers?

A
  • cytochromes
  • Iron-sulfur proteins
25
Q

Cytochromes

A

– Contain a covalently-bound heme

– The heme bound iron atom changes from the ferric (Fe3+) to the ferrous (Fe2+) oxidation state whenever it accepts an electron

26
Q

Iron-sulfur proteins

A

– Sulfur atoms from cysteine side chains within these proteins bind iron in either a 2S:2Fe or 4S:4Fe configuration

27
Q

What are the two mobile electron carriers in the ETC?

A
  • ubiquinone
  • cytochrome C
28
Q

Ubiquinone

A
  • Can carry either one or two electrons
  • Embedded in the membrane via a long chain isoprenoid
  • Helps move proton form matrix to intermembrane space via the Q-cycle
29
Q

Cytochrome C

A
  • A soluble protein with a bound heme prosthetic group
  • Shuttles electrons from cytochrome c reductase to cytochrome oxidase
30
Q

What is ubiquinone (Q) converted to as Hydrogens are added to it?

A
  • 1 H (QH*) = ubisemiquinone
  • 2 H (QH2) = ubiquinol
31
Q

What Are the Three Large Enzyme Complexes in the Respiratory Chain?

A

• NADH Dehydrogenase complex

  • Cytochrome c reductase (b-c1complex)
  • Cytochrome oxidase complex
32
Q

NADH Dehydrogenase complex

A

Accepts electrons from NADH and passes them through flavin and at least 8 ironsulfur centers to ubiquinone

33
Q

Cytochrome C Reductase (complex III)

A
  • Functions as a dimer
  • Each monomer contains 3 hemes bound to cytochromes and an iron-sulfur protein
  • Accepts electrons from ubiquinone and passes them to cytochrome c, one at a time
34
Q

Two-step cytochrome C reductase Q-cycle

A
  • Only one e- can be passed to ubiquinone (Q) at a time
35
Q

Cytochrome oxidase complex (complex IV)

A
  • Functions as a dimer
  • 2 cytochrome hemes and 2 copper atoms
  • Accepts electrons one at a time from cytochrome c
  • Passes electrons four at a time to molecular oxygen
36
Q

The ability of cytochrome oxidase complex to hold onto molecular oxygen until it receive all 4 electrons prevents ____

A

damaging superoxide radical from being released.

37
Q

What is complex II?

A

succinate dehydrogenase

38
Q

Where is complex II?

A

• Complex II is the only membrane bound part of the TCA cycle.

  • The covalently bound FAD accepts two electrons from succinate forming FADH2
  • These electrons move through three iron sulfur clusters to ubiquinone.
39
Q

Beta-oxidation of fatty acids has a much ____ energy yeild than oxidation of glucose

A

higher

31 NADH : 8 NADH

108 ATP : 30 ATP

40
Q

ATP synthase

A
  • F0F1 ATPase
  • Multisubunit integral membrane protein (>500,000 daltons) of the inner mitochondrial membrane
  • Works as a rotary catalyst
  • As protons move through the enzymes, rotational motion is generated.
  • This rotational motion is used to drive protein conformational changes that result in ATP synthesis from ADP and Pi
41
Q

Structure of ATP Synthase?

A
42
Q

ATP synthase dimers assemble ____

A

in cristae

43
Q

Voltage gradient drives:

A

ADP-ATP exchange

44
Q

PH gradient drives:

A

Pyruvate and phosphate import

45
Q

ADP/ATP carrier proteins localize in the ___

A

cristae

46
Q

ATP synthase can work in reverse to pump protons

A
47
Q

_____ uncouple electron transport from ATP synthesis

A
  • Proton ionophores
  • These lipid soluble proton carriers eliminate the proton gradient across the mitochondrial inner membrane
48
Q

Cyanide and carbon monoxide are so toxic because they….

A

inhibit electron transfer in the ETC