Electron Transport Chain Flashcards

1
Q

What is the structure of the Mitochondria?

A
  • Intracellular organelle as big as a bacterium
  • It has two membranes, an inner and outer mitochondrial membrane.
  • It has its own DNA encoding some of the genes required for ETC and other functions
  • Has own transcription and translation machinery, the mitochondrial ribosomes. These are similar to those of bacteria.
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2
Q

Is the oxidation of NADH and FADH2 exergonic or endergonic?

A

The oxidation of these two molecules is extremely exergonic.

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3
Q

What are three ways in which electrons can be transferred?

A
  1. Direct electron transfer (eg. Fe3+ to Fe2+)
  2. Transfer of H atom
  3. Transfer of Hydride ion, as in NADH oxidation to NAD+
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4
Q

What are some membrane-bound electron carriers?

A
  • Ubiquinone or Coenzyme Q
  • Flavoproteins
  • Iron-Sulfur proteins
  • Cytochromes
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5
Q

What are some qualities of Ubiquinone (Coenzyme Q)?

A
  • It is a highly hydrophobic, lipid-soluble benzoquinone with a long isoprenoid side chain.
  • Can accept one electron to become semiubiquinone radical or two electrons to become ubiquinol.
  • can freely diffuse through lipid bilayer, shuttling electrons among less mobile carriers
  • Can carry both electrons and protons, playing a central role in coupling electron flow to proton movement.
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6
Q

What are some qualities of flavoproteins?

A
  • Proteins tightly bound to flavin nucleotides (FMN or FAD)
  • Capable of accepting/donating one or two electrons
  • reduction potential of flavin nucleotides depends on the protein it is bound to.
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7
Q

What are some qualities of Iron-Sulfur Proteins?

A
  • Fe atoms coordinated to Sulfur atoms of either Cys residues of the proteins or also with inorganic sulfur atoms. The Fe is either oxidized or reduced
  • Reduction potential varies depending on microenvironment around Fe atom in the protein.
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8
Q

What are some qualities of Cytochromes?

A
  • Proteins with an Fe-containing heme prosthetic group
  • absorbs light in the visible range due to heme group
  • three classes of cytochromes depending on the heme group they have
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9
Q

What are the differences between the three cytochromes?

A
  • Cytochrome a and b are non-covalently bound to protein, c is covalently bound
  • Cytochrome a and b are membrane proteins whereas cytochrome c in the mitochondria is a soluble protein associated with the outer surface of the membrane by electrostatic interaction
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10
Q

What is complex 1 of the ETC?

A

NADH-Coenzyme Q Oxidoreductase:
largest protein complex in mitochondria (43 polypeptides, 850kDa heavy)
contains 6-7 iron-sulfur clusters and 1 FMN as prosthetic group
Has a binding site for Coenzyme Q, which is a substrate for this complex

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11
Q

What is complex 2 of the ETC?

A

Succinate Dehydrogenase:
Contains 4 different proteins

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12
Q

What is Comlex 3 of the ETC?

A

Cytochrome bc1 Complex or
Ubiquinone: Cytochrome c Oxidoreductase complex.
- Is a dimer of two identical complexes, each containing 11 different subunits.
- The Q cycle occurs within complex 3

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13
Q

What is the Q cycle?

A

Electrons from two electron carriers are transferred throughout complex 3.
- The first electron follows the path
QH2 –>Fe-S->Cyt c1 –>Cyt c
- The second electron follows the path
QH2–>Cyt bL–>cyt bH–>oxidized Q, creating an unstable Q-.
- The Q- ion is converted back into Q by taking 2H+ from the matrix side. The QH2 is then recycled back into the Q cycle.

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14
Q

What is complex 4 of the ETC?

A

Cytochrome c Oxidase:
- Catalyses the transfer of electrons from cyt c to Oxygen, leading to the reduction of Oxygen into H2O
- The complex has 13 subunits and a weight of 240 kDa

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15
Q

What are the three proteins critical for electron flow in Complex 4 of the ETC?

A

Subunits 1,2, and 3:
Subunit 1 contains two heme groups and a Cu ion
Subunit 2 contains two Cu atoms bonded by two sulfur atoms of Cystine
Subunit 3 role is not well understood but critical for complex 4 function

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16
Q

What are the three main Energy Coupling Hypotheses?

A
  1. Chemical Coupling Hypothesis, 1953, Slater
  2. Conformational Coupling Hypothesis, 1964, Boyer
  3. The Chemi-Osmotic Hypothesis, 1961, Mitchell
17
Q

What are the mechanisms of H+ transport?

A
  1. The Redox Loop Mechanism
  2. The Proton Pump mechanism
18
Q

What are the steps of the redox loop mechanism?

A
  • Electron carriers capable of carrying H+ receive electrons from inner side (matrix)
  • And transfers protons to outside during their oxidation by the next carrier which carries electrons (eg. Fe2+)
19
Q

What are the steps in the Proton Pump Mechanism?

A
  • During Oxidation-Reduction reaction in ET chain components
  • reduction causes conformational change, which decreases pKa and exposes side chain to outside
  • H+ is dissociated
  • Reoxidation restores original conformation
20
Q

What is the binding change mechanism for ATP synthesis?

A
  • The translocation of H+ is carried out by F0 while the formation of Phosphoanhydride bond is catalysed by F1
21
Q

What are the three interacting polymers of F1?

A

L State: Binds ADP and Pi loosely
T State: Binds ADP and Pi tightly
O State: Open state, does not bind at all, releases ATP

22
Q

What are the steps in the binding of ADP and Pi to F1?

A
  1. ADP and Pi bond to the “L” site
  2. Free-Energy driven conformational change converts “L” site to a “T” site which catalyses ATP formation. Also involves conversion of ATP containing “T” site to an “O” site.
  3. ATP synthesized on “T” site on one subunit while ATP dissociates from “O” site on another subunit
23
Q

What does uncoupling oxidative phosphorylation mean?

A

Any mechanism that can dissipate the H+ gradient will uncouple the ATP generation

24
Q

What molecules uncouple ATP generation?

A
  • 2,4-Dinitrophenol (DNP)
  • Carbonylcyanide-p-trifluoromethoxy phenyl hydride (FCCP)

Both are lipid-soluble compounds that can transport H+ across inner membrane. They uncouple ATP synthesis

25
Q

How was DNP used in the 1920’s?

A

It was originally used as a diet pill to make ATP synthesis inefficient (wasted NADH by dissipating H+ gradient)
Burned more food without wasting energy
It was extremely toxic and led to the death of many patients

26
Q

What are the drawbacks of aerobic metabolism of glucose?

A
  • Can cause irreversible damage when deprived of O2
  • Risk of free radical damage