14: Energy Conversion: Mitochondria and Chloroplasts Flashcards

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1
Q

Which regions of the mitochondrial membrane contain ATP synthase and the protein complexes of the respiratory chain?

A

The cristae - specialized invaginations of the inner memb.

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2
Q

Name some of the roles of mitochondria in cellular metabolism

A

Buffer the redox potential of the cell (provides electron transfer: NAD+ -> NADH)
- Important in the metabolic adaptation of cells to different nutritional conditions.

Central role in memb. biosynthesis:

  • Produces cardiolipin (two-headed phospholipid) for own inner memb.
  • Produces phosphatidyletanolamine, phosphatidylglycerol, phosphatidic acid

Important calcium buffers, taking up calcium from the ER and sarcoplasmic reticulum

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3
Q

Give a brief description of the processes in the respiratory chain

A
  1. 2e + H+ are removed from NADH->NAD+
  2. 2e passed to an electron carrier in the inner memb.
    • e have large negative redox potential - high energy level - that gradually drops as they pass along the chain.
  3. Three respiratory enz. complexes: each has a higher affinity for electrons than its predecessor.
  4. Molecular oxygen is the final e-acceptor (highest affinity)

Net result: pumping of H+ out of the matrix across the inner memb. driven by the electrically favorable flow of electrons.
=> pH-gradient (highest in matrix) and voltage gradient => memb. potential, neg. in cristae, pos. in crista space

ΔpH + ΔV = electrochemical gradient (~180 mV)
=> proton-motive force, e back into matrix.

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4
Q

What is the path of e-flow in the electron transport chain?

A

NADH → NADH dehydrogenase complex → ubiquinone (coenzyme Q) → cytochrome c reductase → cytochrome c → cytochrome c oxidase complex → molecular oxygen (O2)

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5
Q

What is a redox potential?

A

Affinity for electrons.
Defined as E_0, measured for a std. state where all of the reactants are at a concentration of 1M (E’_0)
Weak affinity (low potential) are useful as carriers/donors.
Redox pair: oxidized/reduced forms of a compound.

Electrons move spontaneously from a redox pair like NADH/NAD+ with a lower redox potential (lower affinity for electrons) to a redox pair like O2/H2O with a higher redox potential.

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6
Q

What are the electron-transfer cofactors of the respiratory chain?

A

Transition ions (Fe, Cu, Ni, Mn) bound to proteins in the complexes.
Cytochromes contain a bound heme group, in which an iron atom is tightly held. 1e at a time.
Iron-sulfur clusters. 1e at a time.

Simplest cofactor: quinone (ubiquinone/coenzyme Q), not always protein-bound. Small hydrophobic molecule that is freely mobile in the lipid bilayer. Donate 1 or 2e. Picks up a proton from water with each electron when reduced.

Mitochondrial e-transport chain:

  • 6 cytochrome hemes
  • 8 iron-sulfur clusters
  • 3 copper atoms
  • 1 flavin mononucleotide
  • ubiquinone

Iron-sulfur dominates at the start (low e affinity).
Heme cytochromes dominate at the 2nd half.

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7
Q

What is the contribution of NADH dehydrogenase to the proton gradient?

A

NADH -> 2e is transferred in the matrix arm via monoflavin nucleotide and iron-sulfur clusters.
2e reduces quinone (Q->QH2), giving energy to the transfer of 4H+ into the crista space.

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8
Q

How are protons transferred from NADH dehydrogenase to cytochrome c reductase and further?

A

Via quinone and the Q cycle.
Cyt C reductase has a binding site for a 2nd QH.
1e transferred through cyt c red. to the carrier protein cytochrome c.
1e is recycled back into the quinone pool

=> for every e that is transferred from NADH dehydrogenase to cytochrome c, 2 protons are pumped out of the matrix.

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9
Q

What is the role of cytochrome c oxidase in the electron-transport chain?

A

Binds O2 at bimetallic center clamped between a heme-linked Fe atom and a Cu atom until it has picked up 2e.
Prevents the formation of radicals.
Release of 2H2O
Enables 90% of O2 uptake in most cells.

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10
Q

What is the advantage of the supercomplex in the crista membrane? What lipid holds the components together?

A

Help the mobile electron carriers ubiquinone (crista memb.) and cytochrome c (crista space) transfer electrons with high efficiency.

Cardiolipin

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11
Q

How can ATP synthase produce ATP when it is an energetically unfavorable process?

A

Allosteric shape changes in ATP synthase couple ATP synthesis (energetically unfavorable) directly to the energetically favorable flow of protons across its memb.

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12
Q

What is the ATP yield from the complete oxidation of one glucose molecule?

A

30 ATP (theoretically)

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