Day 41 Flashcards

1
Q

Thermodynamics of Electron Transport

A
  • Oxygen is the final electron receptor for both NADH and FADH2
  • Remember that electron affinity increases with standard reduction potential
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2
Q

ETC Sequence of Transport

A
  • electrons passed from NADH and FADH2 to Complex 1 and Complex 2 respectively
  • those electrons are then carried by Coenzyme Q (CoQ or ubiquinone) to Complex 3
  • Complex 3 electrons are then carried by a peripheral membrane known as Cytochrome C to Complex 4
  • Each complex catalyzes the redox reaction of electron transfer from one molecule to another - Complex 4 catalyzes electron transfer from cytochrome c to oxygen
  • Transversing of electrons through Complex 1,3, and 4 power the synthesis of ATP
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3
Q

Complex 1 Inhibitors

A
  • Rotenone (plant toxin)
  • Amytal )barbiturate
  • they both block the electrons from transporting though
  • ALLLL complex inhibitors block oxygen consumption because no use for final electron accepter
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4
Q

Complex 3 Inhibitors

A

Antimycin A (antibiotic)

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5
Q

Complex 4 Inhibitors

A

Cyanide

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6
Q

More fun complex facts

A
  • Each protein complex in the ETC have prosthetic groups capable of redox activity
  • They all laterally mobile in the membrane and don’t form a higher stable structure ( not even present in equimolar amounts)
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7
Q

Complex 1

A

Name: NADH-CoQ Oxidoreductase

  • L-shaped with one arm in membrane other in matrix
  • has flavin thing like FAD but no AMP moiety 6-7iron/sulfer clusters
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8
Q

Complex 1 Coenzymes

A

1) Iron-Sulfur Cluster
- [2Fe-2S] and [4Fe-4s] but both have 4 cysteine sulfhydryls
- Cluster can undrgo one-electron redox reactions
2) FMN and CoQ
- together have three oxidation states (fully oxidized, semiquinone, fully reduced)
- Both can accept two or one electron
- FMN is tightly bound to proteins while CoQ has a hydrophobic tail and is soluble in lipid bilayer

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9
Q

Electron Transport in Complex 1

A
  • transit of electrons from NADH to CoQ is probably stepwise
  • must involve reduction of each group as it binds electrons followed by oxidation as it passes the electrons along to the next group
  • electrons can “jump” 14angstrums cuz quantum mechanics so redox centers don’t have to touch
  • NADH can only give 2 electrons but cytochromes can only participate in 1 electron transfers…..so there are the two initial electron carriers FMN and CoQ to go from NADH trying to give 2 e to a 1e cytochrome
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10
Q

Proton Translocation

A
  • during electron transfer in Complex 1, 4 protons go into intermembrane space
  • we don’t know how pumping works but pK values of side chains are probs altered
  • Protons “hop” along a chain of hydrogen bonded groups unlike other ions.
  • bacteriorhodopsin is light driven proton pump. When retinal changes, the protein conformation and pK change of a protein channel
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11
Q

Complex 2

A

Name: Succinate-CoQ Oxidoreductase

  • has enzyme succinate dehydrogenase (like the CAC with that FAD cofactor)
  • has 3 iron-sulfur clusters and cytochrom b560 that comes with a heme group with reaction iron center
  • Transport of electrons from succinate to CoQ DOES NOT MAKE ATP NOT SEQUENTIAL
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12
Q

Complex 3

A

Name: CoQ-Cytochrom c Oxidoruductase

  • passes electrons from reduced CoQ to cytochrome c
  • has two b-type cytochromes, one cytochrome c1, and one iron-sulfur cluster that is coordinated by histidines know as Rieske Center
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13
Q

The Q Cycle

A
  • Electron transport and proton pumping in complex 3
  • CoQH2 is an electron carrier that will permit two electrons to be carried in ordre to reduce two molecules of cytochrome c which is a one elecron carrier
  • Occurs by a split in the electrons where one goes to cytochrome c and one goes to cytochrome b in a cyclic manner
  • CoQH2 goes through a two cycle reoxidation where it froms a stable radical as an intermediate
  • two independent binding sites. Qo–CoQH2 and Qi—CoQ’ and CoQ
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14
Q

Cytochrome C

A
  • electrons in cytochrome c1 are transferred to cytochrome c which is a peripheral membrane protein the the intermembrane space
  • shuttles electrons from Com3 to Com4
  • just like to other cytochromes, have redox-reactive iron coordinated in bound heme group
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15
Q

Complex 4

A

Name: Cytochrome c Oxidase

  • catalyzes the 1-electron oxidations of four consecutive reduced cytochrome c molecules and the 4 electron reduction of one O2 molecules
  • 4 redox centers; cytochrome a, cytochrome a3, a copper atom known as CuB, and a pair of copper atoms knows as the CuA center
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16
Q

Oxygen Reduction by Complex 4

A
  • reduction of oxygen to water by complex 4 occurs at the a3-CuB binuclear complex and requires 4 electrons
  • Fully reduced Fe(II)-Cu(1) complex can only donate a total of three electrons so the fourth comes from tyrosine244 in transiently forming a tyrosyl radical
17
Q

Complex 4 and Proton Translocation

A
  • 4 protons are taken up from the matrix during oxygen reduction to yield 2 waters
  • that is coupled to the translocation of 4 pumped protons from the matrix, making proton gradient
  • each turnover of cytochrome c oxidase (complex 4) makes 8 positive charges be transported across membrane and contributes to the membrane potential
  • The K Channel - (required Lys residue) leads from the matrix to Tyr244 but isn’t connected to intermembrane space
  • The D Channel - (required Asp residue) connects from matrix to binuclear center, where it connects with the exit channel that’s open to intermembrane space. The D is required for proton involved in second part of the reaction cycle and the proton gradient