Electron Transport Chain (ETC)
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Questions and Answers

What is the primary role of Coenzyme Q in the electron transport chain?

  • To pump protons across the inner mitochondrial membrane.
  • To directly oxidize NADH.
  • To act as a mobile carrier of electrons between protein complexes. (correct)
  • To directly reduce oxygen to form water.

Which of the following describes the flow of electrons through Complex I?

  • FMN → NADH → Fe-S → UQ
  • NADH → FMN → UQ → Fe-S
  • NADH → FMN → Fe-S → UQ (correct)
  • NADH → UQ → FMN → Fe-S

What is the net effect of Complex II activity on the electron transport chain?

  • Pumping protons from the cytosol to the matrix.
  • Reducing ubiquinone and pumping protons.
  • Oxidizing succinate and reducing ubiquinone. (correct)
  • Oxidizing FADH2 and reducing NADH.

Which enzyme directly links the TCA cycle to the electron transport chain by supplying electrons to Coenzyme Q?

<p>Succinate dehydrogenase. (D)</p> Signup and view all the answers

How does electron transfer in Complex I contribute to the establishment of a proton gradient?

<p>By transporting protons from the matrix to the cytosol. (A)</p> Signup and view all the answers

Which component of Complex II directly reduces ubiquinone (CoQ)?

<p>Iron-sulfur clusters. (D)</p> Signup and view all the answers

What is the role of the long helical rod (HL) in Complex I during electron transfer?

<p>To facilitate conformational changes that contribute to proton translocation. (C)</p> Signup and view all the answers

In addition to Complex II, what other enzymes supply electrons to ubiquinone (CoQ)?

<p>Both B and C (D)</p> Signup and view all the answers

Which subunits are typically found in most organisms and are sufficient for both oxygen reduction and proton transport?

<p>Subunits I, II, and III (C)</p> Signup and view all the answers

What is the function of cytochrome c oxidase (Complex IV) in the electron transport chain?

<p>Transfers electrons from cytochrome c to reduce oxygen on the matrix side (B)</p> Signup and view all the answers

What is the potential advantage of electron transport complexes forming supercomplexes (respirasomes)?

<p>Supercomplexes may represent functional states that are advantageous for the organism (C)</p> Signup and view all the answers

According to the chemiosmotic hypothesis proposed by Peter Mitchell, what directly drives ATP synthesis?

<p>A proton gradient across the inner mitochondrial membrane (C)</p> Signup and view all the answers

In the model for the electron transport pathway, what is the role of ubiquinone (UQ/UQH2) and cytochrome c (cyt c)?

<p>They are mobile carriers that transfer electrons between the complexes (A)</p> Signup and view all the answers

What was the traditional view of how electron transport chain complexes functioned before the discovery of supercomplexes?

<p>They were thought to exist and function independently in the mitochondrial inner membrane (C)</p> Signup and view all the answers

What critical evidence did Stoeckenius and Racker provide in their experiment to support the Mitchell chemiosmotic hypothesis?

<p>They showed that artificial vesicles containing bacteriorhodopsin and ATP synthase could synthesize ATP when exposed to light. (A)</p> Signup and view all the answers

In the context of the electron transport chain and ATP synthesis, what does the term 'chemiosmotic' refer to?

<p>The use of an electrochemical gradient of protons to drive ATP synthesis (D)</p> Signup and view all the answers

In chemiosmotic coupling, what two components contribute to the free energy difference for protons across the inner mitochondrial membrane?

<p>Concentration difference and electrical potential (A)</p> Signup and view all the answers

Which of the following best describes the function of the F0 component of ATP synthase?

<p>It forms a transmembrane channel through which protons move, driving ATP synthesis. (A)</p> Signup and view all the answers

Which subunits constitute the rotating portion (rotor) of the ATP synthase motor?

<p>c, γ, and ε (B)</p> Signup and view all the answers

According to Boyer's binding change mechanism, what is the state of the three β-subunits of F1 at any given instant?

<p>The three subunits exist in three different conformations, representing three sequential steps of ATP synthesis. (C)</p> Signup and view all the answers

How does the rotation of the c-ring in ATP synthase contribute to ATP synthesis?

<p>The rotation of the c-ring drives conformational changes in the α- and β-subunits of F1 that synthesize ATP. (A)</p> Signup and view all the answers

What is the role of the a-subunit in the F0 complex of ATP synthase?

<p>It contains half-channels for proton entry and exit from the c-ring. (C)</p> Signup and view all the answers

How was it demonstrated that a proton gradient is sufficient to drive ATP synthesis?

<p>By illuminating bacteriorhodopsin-containing vesicles and observing ATP synthesis. (B)</p> Signup and view all the answers

In a redox reaction, if substance A has a more negative standard reduction potential ($\varepsilon$o) than substance B, which statement is correct?

<p>Substance A is more likely to be oxidized and is a stronger reducing agent than substance B. (B)</p> Signup and view all the answers

Which of the following is NOT a function of the F1 component of ATP synthase?

<p>Forming a channel for proton translocation across the membrane (B)</p> Signup and view all the answers

Consider a hypothetical redox reaction where compound X reduces compound Y. Given their standard reduction potentials are $\varepsilon$o(X) = -0.25 V and $\varepsilon$o(Y) = +0.15 V, what is the standard cell potential ($\Delta\varepsilon$o) for the overall reaction?

<p>0.40 V (C)</p> Signup and view all the answers

The Nernst equation describes the relationship between cell potential and reaction quotient. Which scenario would result in a cell potential equal to the standard cell potential ($\varepsilon = \varepsilon$o)?

<p>When the reaction quotient (Q) is equal to 1. (B)</p> Signup and view all the answers

In a concentration cell, voltage is generated based on differences in concentration. For a cell with Zn/Zn2+ half-cells at different concentrations, which change would increase the cell potential?

<p>Increasing the concentration of Zn2+ in the anode compartment. (B)</p> Signup and view all the answers

In the electron transport chain, electrons are passed between various protein complexes. What role do coenzyme Q (ubiquinone) and cytochrome c play?

<p>They serve as mobile electron carriers between complexes. (B)</p> Signup and view all the answers

Given the following half-reactions and their standard reduction potentials:

$NAD^+ + 2H^+ + 2e^- \rightarrow NADH + H^+ \varepsilon o' = -0.32V$ $\frac{1}{2}O_2 + 2H^+ + 2e^- \rightarrow H_2O \varepsilon o' = +0.816V$

What is the standard free energy change ($\Delta Go'$) for the oxidation of NADH by oxygen?

<p>-219 kJ/mol (B)</p> Signup and view all the answers

During the transfer of electrons down the electron transport chain, energy is released. What is the general trend regarding the energy levels of electrons as they move through the chain?

<p>Electrons lose energy as they move from Complex I/II to Complex IV. (D)</p> Signup and view all the answers

In the citric acid cycle, isocitrate is converted to $\alpha$-ketoglutarate, coupled with the reduction of $NAD^+$ to NADH. Given the following reduction potentials:

$NAD^+ + 2H^+ + 2e^- \rightleftharpoons NADH + H^+ \varepsilon o' = -0.32V$ $\alpha-Ketoglutarate + CO_2 + 2e^- \rightleftharpoons Isocitrate \varepsilon o' = -0.38V$

What is the $\Delta Go'$ for this reaction?

<p>$-11.58 kJ/mol$ (B)</p> Signup and view all the answers

In the context of ATP synthase, what is the primary role of the flow of protons?

<p>To drive the rotation of the rotor and induce conformational changes in the β subunits, leading to ATP synthesis. (A)</p> Signup and view all the answers

According to Boyer's binding change mechanism, what are the three distinct conformational states of the active sites in the F1 portion of ATP synthase?

<p>Open (O), Loose (L), and Tight (T). (A)</p> Signup and view all the answers

How does rotenone, a known inhibitor, affect the electron transport chain?

<p>It blocks the transfer of electrons in Complex I. (C)</p> Signup and view all the answers

Cyanide is a potent inhibitor of oxidative phosphorylation. What is its specific mechanism of action?

<p>It competes with oxygen and binds tightly to the ferric form (Fe3+) of a3 in Complex IV. (B)</p> Signup and view all the answers

Oligomycin is an inhibitor that directly targets:

<p>ATP synthase. (B)</p> Signup and view all the answers

Which of the following drugs has been shown to inhibit Complex I of the electron transport system?

<p>Rotenone (C)</p> Signup and view all the answers

What is the effect of Amytal on the electron transport chain?

<p>It inhibits Complex I, similar to rotenone. (B)</p> Signup and view all the answers

How would blocking Complex I directly impact ATP synthesis?

<p>ATP synthesis would decrease as fewer electrons are passed to ubiquinone, reducing the proton gradient. (A)</p> Signup and view all the answers

What is the primary role of the Q cycle in Complex III of the electron transport chain?

<p>To facilitate the transfer of electrons from CoQ to cytochrome c, coupled with proton pumping. (B)</p> Signup and view all the answers

Which of the following statements accurately describes the roles of ubiquinol (UQH2) and cytochrome c in the electron transport chain?

<p>UQH2 is a lipid-soluble carrier, while cytochrome c is a water-soluble carrier. (B)</p> Signup and view all the answers

Cytochrome c oxidase (Complex IV) uses electrons from cytochrome c to catalyze which of the following reactions?

<p>The four-electron reduction of $O_2$ to $2H_2O$. (C)</p> Signup and view all the answers

What is the role of the hemes $b_L$ and $b_H$ within the b cytochrome of Complex III?

<p>They facilitate one-electron transfers as part of the Q cycle. (C)</p> Signup and view all the answers

How many protons are translocated across the inner mitochondrial membrane by Cytochrome c oxidase (Complex IV) during each catalytic cycle?

<p>Four protons are used to reduce oxygen and four protons are pumped. (B)</p> Signup and view all the answers

In Complex IV, what is the final destination of electrons that originate from cytochrome c?

<p>They are used to reduce $O_2$, forming $H_2O$. (B)</p> Signup and view all the answers

Cytochrome c contains a heme group with a central iron atom. What is the function of this iron atom?

<p>It facilitates electron transfer by cycling between $Fe^{2+}$ and $Fe^{3+}$ states. (C)</p> Signup and view all the answers

Which of the following is a critical characteristic that allows cytochrome c to function effectively in the electron transport chain?

<p>Its water-soluble nature, allowing it to move between Complex III and Complex IV. (D)</p> Signup and view all the answers

Within Complex I, what is the correct sequence of electron transfer between the following components?

<p>NADH → FMN → Fe-S → UQ → Fe-S (D)</p> Signup and view all the answers

What is the net number of protons that Complex I translocates across the inner mitochondrial membrane for every two electrons transferred from NADH to Coenzyme Q?

<p>Four H+ (C)</p> Signup and view all the answers

In Complex II, what is the immediate electron acceptor from FADH2 generated during succinate oxidation?

<p>Iron-Sulfur (Fe-S) clusters (C)</p> Signup and view all the answers

Why is Complex II unable to directly contribute to the proton gradient across the inner mitochondrial membrane, unlike Complexes I, III, and IV?

<p>The free energy change associated with electron transfer is insufficient. (B)</p> Signup and view all the answers

How do fatty-acyl CoA dehydrogenases contribute to the electron transport chain?

<p>They transfer electrons from fatty acyl-CoA to FAD, then to ubiquinone. (C)</p> Signup and view all the answers

How does the conformational change in the long helical rod (HL) of Complex I facilitate proton translocation?

<p>It reorients charged amino acid residues, enabling proton transfer. (C)</p> Signup and view all the answers

Which of the following best describes the function of the Fe-S clusters in both Complex I and Complex II of the electron transport chain?

<p>They facilitate the transfer of electrons between FMN/FADH2 and Coenzyme Q. (B)</p> Signup and view all the answers

Which component of Complex II is covalently bound?

<p>FAD (B)</p> Signup and view all the answers

What is the net outcome of the Q cycle in Complex III regarding the oxidation and reduction of Coenzyme Q (CoQ) and Cytochrome c?

<p>Net oxidation of 1 CoQH2 and reduction of 2 Cyt c. (C)</p> Signup and view all the answers

Within Complex III, what is the specific role of the b cytochrome, particularly with its hemes $b_L$ and $b_H$?

<p>To mediate electron transfer between ubiquinone and cytochrome c. (D)</p> Signup and view all the answers

Why is ubiquinol (UQH2) a suitable electron carrier within the inner mitochondrial membrane?

<p>It is lipid-soluble, enabling it to diffuse through the hydrophobic environment of the membrane. (B)</p> Signup and view all the answers

How does the structure of cytochrome c facilitate its role as a mobile electron carrier?

<p>It is a small, water-soluble protein that can move freely in the intermembrane space. (C)</p> Signup and view all the answers

What distinguishes cytochromes from other electron carriers like Fe-S clusters in the electron transport chain regarding their electron transfer capabilities?

<p>Cytochromes and Fe-S clusters are both one-electron transfer agents. (A)</p> Signup and view all the answers

What is the final electron acceptor in the electron transport chain, and what product is formed by its reduction?

<p>Oxygen, producing water ($H_2O$). (B)</p> Signup and view all the answers

Besides reducing oxygen to water, what other crucial function does cytochrome c oxidase (Complex IV) perform to contribute to the proton gradient?

<p>It transports protons across the inner mitochondrial membrane. (D)</p> Signup and view all the answers

How many protons are directly involved in the reduction of one molecule of oxygen by Cytochrome c oxidase (Complex IV), and how many protons are translocated across the inner mitochondrial membrane during this process?

<p>Four protons participate in O2 reduction, and four protons are translocated. (D)</p> Signup and view all the answers

What is the functional significance of the three largest subunits (I, II, and III) that are common to most organisms in the context of Complex IV?

<p>They catalyze the reduction of oxygen, establishing a proton gradient and housing redox centers. (A)</p> Signup and view all the answers

How does cytochrome c interact with Complex IV to facilitate electron transfer?

<p>It binds on the cytosolic face, transferring electrons through copper and heme centers to reduce oxygen on the matrix side. (A)</p> Signup and view all the answers

What advantage do supercomplexes (respirasomes) potentially offer over independently functioning electron transport chain complexes?

<p>Supercomplexes might offer enhanced efficiency in electron transfer and substrate channeling compared to individual complexes. (D)</p> Signup and view all the answers

What is the primary role of ubiquinone ($UQ/UQH_2$) and cytochrome c (cyt c) in the electron transport pathway?

<p>They act as mobile carriers, shuttling electrons between the complexes. (A)</p> Signup and view all the answers

What fundamental principle did Peter Mitchell propose to explain the coupling of oxidation and phosphorylation in ATP synthesis?

<p>A proton gradient across the inner mitochondrial membrane drives ATP synthesis. (D)</p> Signup and view all the answers

According to the chemiosmotic hypothesis, how is the proton gradient generated by the electron transport chain utilized to produce ATP?

<p>The potential energy stored in the proton gradient is converted into chemical energy as protons flow back across the membrane through ATP synthase. (A)</p> Signup and view all the answers

What was the key finding of the Stoeckenius and Racker experiment that supported the chemiosmotic hypothesis?

<p>They showed that artificial vesicles containing bacteriorhodopsin and ATP synthase could synthesize ATP when exposed to light. (A)</p> Signup and view all the answers

In the experiment conducted by Stoeckenius and Racker, which two components were reconstituted into artificial vesicles to demonstrate the chemiosmotic hypothesis?

<p>ATP synthase and bacteriorhodopsin (C)</p> Signup and view all the answers

How do uncouplers directly affect the electron transport chain and ATP synthesis?

<p>They disrupt the proton gradient, allowing electron transport to continue without ATP synthesis. (A)</p> Signup and view all the answers

Why is the movement of ATP out of the mitochondria and ADP into the mitochondria considered equivalent to the movement of a proton into the matrix?

<p>Because the exchange results in a net movement of negative charge out of the matrix, which is electrically equivalent to a proton moving in. (C)</p> Signup and view all the answers

What is the effect of uncoupling agents on the rate of oxygen consumption in the mitochondria?

<p>Oxygen consumption increases as the electron transport chain attempts to maintain the proton gradient. (A)</p> Signup and view all the answers

How does the ATP-ADP translocase contribute to the overall proton motive force required for ATP synthesis?

<p>It consumes a portion of the proton gradient by exchanging ATP for ADP. (C)</p> Signup and view all the answers

What is the P/O ratio when electrons from FADH2 (produced by succinate dehydrogenase) enter the electron transport chain?

<p>1.5 ATP per oxygen atom reduced. (C)</p> Signup and view all the answers

How does the cellular location of NADH (cytosolic vs. mitochondrial) affect its contribution to ATP synthesis, and what mechanisms facilitate the use of cytosolic NADH for oxidative phosphorylation?

<p>Shuttle systems indirectly transfer electrons from cytosolic NADH to mitochondrial carriers. (A)</p> Signup and view all the answers

During hibernation, animals uncouple oxidative phosphorylation to generate heat. What is the most direct mechanism by which this uncoupling increases heat production?

<p>Protons leak across the inner mitochondrial membrane, releasing energy as heat. (A)</p> Signup and view all the answers

Imagine an experiment where the ATP-ADP translocase is inhibited. What would be the MOST immediate consequence within the mitochondria?

<p>Buildup of ADP in the mitochondrial matrix and decreased ATP levels. (C)</p> Signup and view all the answers

How does the electrochemical gradient of protons across the inner mitochondrial membrane store energy?

<p>By establishing both a concentration difference and an electrical potential, both of which contribute to the free energy difference. (C)</p> Signup and view all the answers

Which component of the ATP synthase complex forms the channel through which protons flow to drive ATP synthesis?

<p>The F0 component, specifically the a, b, and c subunits. (C)</p> Signup and view all the answers

What role do the a- and b-subunits play in the F0 component of ATP synthase?

<p>They constitute part of the stator, providing a stationary framework that supports the rotation of the c-ring. (D)</p> Signup and view all the answers

How does the rotation of the c-ring in ATP synthase facilitate ATP synthesis?

<p>By causing conformational changes in the $\alpha$- and $\beta$-subunits of $F_1$, leading to ATP synthesis. (C)</p> Signup and view all the answers

According to Boyer's binding change mechanism, what is the relationship between the three $\beta$-subunits of F1 at any given moment?

<p>The three $\beta$-subunits exist in three different conformations, each corresponding to a different step or state in ATP synthesis. (B)</p> Signup and view all the answers

In the context of the rotating molecular motor of ATP synthase, what is the role of the stalk formed by the b-, d-, and h-subunits?

<p>To connect the F0 component in the membrane to the F1 component, acting as a bridge. (A)</p> Signup and view all the answers

How do protons move from the inlet half-channel to the outlet half-channel in the a-subunit of ATP synthase?

<p>Protons are transferred to binding sites on c-subunits, and the rotation of the c-ring delivers them to the outlet half-channel. (D)</p> Signup and view all the answers

What is the immediate consequence of proton entry into the inlet half-channel of the a-subunit in ATP synthase?

<p>Binding of protons to specific sites on the c-subunits of the F0 component. (D)</p> Signup and view all the answers

According to Boyer's binding change mechanism, how do the three active sites in the F1 portion of ATP synthase function?

<p>They cycle through distinct conformations (open, loose, and tight) with varying affinities for ligands in a coordinated manner to drive ATP synthesis. (B)</p> Signup and view all the answers

How does the flow of protons through ATP synthase contribute to ATP production?

<p>It drives conformational changes in the β subunits of the F1 portion, facilitating the binding of ADP and Pi and the release of ATP. (D)</p> Signup and view all the answers

What is the significance of John Walker's determination of the F1 portion structure of ATP synthase?

<p>It provided structural evidence supporting Boyer's binding change mechanism by showing distinct conformations of the β subunits. (D)</p> Signup and view all the answers

How does rotenone, a common inhibitor, affect the electron transport chain and ATP synthesis?

<p>It blocks electron transfer in Complex I, reducing the proton gradient and ATP synthesis. (A)</p> Signup and view all the answers

How do cyanide, azide, and carbon monoxide (CO) inhibit the electron transport chain?

<p>By inhibiting Complex IV, binding tightly to the $Fe^{3+}$ form of $a_3$, blocking the transfer of electrons to oxygen. (C)</p> Signup and view all the answers

What is the specific mechanism by which oligomycin inhibits ATP synthase?

<p>It inhibits the rotation of the c-ring in the $F_0$ subunit, preventing proton translocation. (C)</p> Signup and view all the answers

Which complex of the electron transport chain is targeted by Amytal and Demerol?

<p>Complex I (A)</p> Signup and view all the answers

How may a naturally occurring substance such as rotenone, be useful as an inhibitor of Complex I?

<p>It can be used to selectively paralyze fish, aiding in their capture. (A)</p> Signup and view all the answers

Flashcards

Coenzyme Q

A mobile electron carrier that participates in the electron transport chain.

Complex I

Also known as NADH-CoQ Reductase or NADH dehydrogenase, it catalyzes electron transfer from NADH to Coenzyme Q.

Electron Path in Complex I

NADH → FMN → Fe-S → UQ → FeS → UQ

Proton Transport by Complex I

Complex I moves four protons (H+) from the matrix to the intermembrane space per two electrons transferred

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Complex II

Also known as Succinate-CoQ Reductase or succinate dehydrogenase, it catalyzes electron transfer from succinate to Coenzyme Q.

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Electron Path in Complex II

succinate → FADH2 → 2Fe2+ → UQH2

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Fatty-Acyl-CoA Dehydrogenases

Enzymes involved in fatty acid oxidation that contribute electrons to ubiquinone (UQ).

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Proton Pumping by Complex II

Complex II does not pump protons, which means less energy for H+ pumping.

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Redox Potential (â„°o)

A measure of the tendency of a chemical species to acquire electrons and thereby be reduced.

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Maximum Positive Voltage

Maximum positive voltage is achieved with the most negative ΔG0. In a redox reaction, inverting the bottom reaction and adding both gives the maximum positive voltage

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Nernst Equation

ΔG =ΔG0 + RTLnQ, ΔG = -nF Δɛ, ΔG0= -nF Δɛ0, Δɛ = Δɛ0 –RT/nFLnQ

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Concentration Cell

Voltage generated by concentration differences of ions. Requires the same material on both half-cells (Δɛ0 =0).

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Electron Flow in ETC

Electrons generally fall in energy through the chain from complexes I and II to complex IV

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ETC Components

Four protein complexes in the inner mitochondrial membrane. A lipid-soluble coenzyme (ubiquinone [UQ], also known as Coenzyme Q [CoQ]) and a water-soluble protein (cytochrome c) shuttle between protein complexes.

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Coenzyme Q (CoQ)

Mobile electron carrier that shuttles electrons between complexes in the electron transport chain.

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ΔG' Calculation

ΔG' = -nFΔɛo'. For one NADH to H2O, ΔGo‘ = -219 kJ/mol (or about 7 ATPs), but in reality about 3 ATPs formed.

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Complex IV Function

Transfers electrons from cytochrome c to reduce oxygen on the matrix side of the inner mitochondrial membrane.

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Supercomplexes

Multimeric assemblies of electron transport chain complexes. Also known as respirasomes.

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UQ/UQH2 and Cyt c

Mobile carriers that transfer electrons between the complexes.

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Mitchell Hypothesis

Electron transfer energy is stored in a proton gradient across the inner mitochondrial membrane.

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Proton Gradient

The proton and electrochemical gradients existing across the inner mitochondrial membrane.

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Racker and Stoeckenius Experiment

Artificial vesicles used to confirm the chemiosmotic hypothesis.

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Complex I Subunits

Contains the proton channels and the redox centers.

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Chemiosmotic Hypothesis

A gradient resulted in a protein motive force.

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Q cycle

A unique redox cycle in Complex III where CoQ passes electrons to cytochrome c.

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b cytochrome

The principal transmembrane protein in Complex III, containing hemes bL and bH.

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Cytochrome c

Water-soluble electron carrier that receives electrons from Complex III.

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Oxygen (O2)

The final electron acceptor in the electron transport pathway, reduced to water by Complex IV.

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hemes a and a3 and copper sites

Two types of metal-containing sites found in Cytochrome c Oxidase (Complex IV).

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Cytochrome c Oxidase

The enzyme complex that transfers electrons from cytochrome c to oxygen, reducing it to water, while also transporting H+ across the inner mitochondrial membrane.

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F1 portion of ATP synthase

ATP synthase component containing three catalytic β subunits

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Binding change mechanism

Mechanism where ATP synthesis is driven by conformational changes in the β subunits of ATP synthase.

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Rotenone

Inhibits Complex I of the electron transport system, paralyzing fish.

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Cyanide, Azide, CO

Block Complex IV in oxidative phosphorylation by binding to Fe3+.

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Oligomycin

An ATP synthase inhibitor that blocks the flow of protons.

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Amytal

A barbiturate, inhibits Complex I of the electron transport system.

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Demerol

Inhibits Complex I of the electron transport system.

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ATP Synthase

Enzymatic complex that synthesizes ATP using the proton gradient generated by the electron transport chain.

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Bacteriorhodopsin

A transmembrane protein that pumps protons across the membrane using light energy.

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Electrochemical Gradient

Energy stored in a combination of a chemical gradient and an electrical potential across a membrane.

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F0 Subunit

The membrane-embedded portion of ATP synthase that forms a channel, allowing protons to flow through.

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F1 Subunit

The soluble portion of ATP synthase containing the catalytic sites for ATP synthesis

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c-ring

A ring of subunits within F0 that rotates as protons flow through it, driving ATP synthesis.

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Rotor

The rotating part of the ATP synthase, consisting of the c-ring and central stalk subunits.

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Stator

The non-rotating part of the ATP synthase that supports the F1 and F0 components.

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Oxygen's Role

The final electron acceptor in the electron transport pathway, reduced to water by Complex IV.

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Cytochrome c Binding Site

Cytochrome c binds here to transfer electrons.

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NADH-CoQ Reductase (Complex I)

Transfers electrons from NADH to Coenzyme Q (UQ).

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Complex I Composition

A complex with 44 protein subunits that transfers electrons from NADH to Coenzyme Q.

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Complexes I, II, and III

The minimal complex is sufficient to carry out both oxygen reduction and proton transport

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Respirasomes

Assemblies of multiple electron transport chain complexes.

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Succinate-CoQ Reductase (Complex II)

Transfers electrons from succinate to Coenzyme Q (UQ).

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UQ/UQH2 and Cytochrome c

Mobile carriers that shuttle electrons between complexes.

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Racker and Stoeckenius

Confirmed chemiosmotic hypothesis.

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Bacteriorhodopsin Function

A transmembrane protein that, when illuminated, pumps protons into vesicles.

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Electrochemical Gradient Energy

The free energy stored in a proton gradient, accounting for both concentration and electrical potential differences.

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Proton Gradient Equation

ΔG = ZℱΔψ. Includes terms for concentration difference and electrical potential.

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ATP Synthase Components

Two main parts of ATP synthase; part of the channel, and the catalytic unit.

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F1 Composition

Five polypeptide subunits that make up the soluble catalytic portion of ATP synthase.

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F0 Composition

Hydrophobic subunits that that forms the transmembrane pore of ATP synthase.

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ATP Synthase Rotor

The rotating part of ATP synthase, consisting of c-ring, gamma and epsilon subunits.

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Boyer's Binding Change Mechanism

Describes how the three catalytic sites on ATP synthase cycle through conformations to synthesize ATP.

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Walker’s crystal structure of F1

A structure that contains three states of Boyer’s model

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Proton Flow in ATP Synthase

The flow of protons through ATP synthase causes physical rotation, which drives ATP production.

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Uncouplers of ETC

Molecules that disrupt the tight coupling between electron transport and oxidative phosphorylation by dissipating the proton gradient.

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How uncouplers work

Hydrophobic molecules carrying protons across the mitochondrial membrane, dissipating the proton gradient.

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Heat Generation by Uncoupling

Animals (like hibernating bears) use uncoupling to generate heat by dissipating the proton gradient, bypassing ATP synthase.

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ATP-ADP Translocase

Transports ATP out of the mitochondrial matrix and ADP into the matrix.

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Charge difference

The outside (cytosol) is positively charged relative to the inside.

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ATP-ADP Translocase Cost

The movement of ATP out and ADP in results in a net movement of a negative charge out.

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P/O Ratio

Ratio of ATP molecules produced per pair of electrons moving through the electron transport chain.

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P/O Ratio Calculation (NADH)

Electron transport chain pumps 10 H+ out per electron pair from NADH to oxygen. To move each ATP to cytosol 4 H+ flow back into matrix.

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