BCH 210 (Electron Transport chain)
The Electron Transport Chain Overview
Date: February 19, 2003
Presenter: Bryant Miles
Citric Acid Cycle and Electron Transport
The citric acid cycle oxidizes acetate into:
2 molecules of CO2
Captures electrons as:
3 NADH molecules
1 FADH2 molecule
Reduced molecules (NADH, FADH2) contain high transfer potential electrons.
Electrons are transferred to O2 to form H2O.
Major energy source for ATP production through oxidative phosphorylation.
Free Energy Changes
Standard free energy change for the reaction:
NADH + H+ + 1/2 O2 → NAD+ + H2O
Reduction potentials:
NAD+/NADH: E° = -0.315 V
O2/H2O: E'° = +0.816 V
Overall change in reduction potential:
ΔE'° = +0.816 - (-0.315) = +1.136 V
ΔG° = -nFΔE'° = -219 kJ/mol
ATP synthesis calculation:
ATP = 219 / 30.5 = 7.2 ATP
Mitochondrial Structure
Mitochondria
Sites of electron transport and oxidative phosphorylation.
Eukaryotic cells (e.g., mammalian cells) have mitochondrial structures.
Mammalian cells contain 800 to 2,500 mitochondria each.
Exception: Red blood cells lack mitochondria.
Membrane Structure
Outer membrane:
Contains porins (transmembrane proteins) that allow <10,000 Da molecules to diffuse freely.
Chemically equivalent to the cytosol.
Inner membrane:
Contains 80% proteins contributing to electron transport and ATP synthesis.
Impermeable to ions and molecules; requires transport proteins for crossing.
Folded into cristae, increasing surface area.
Matrix:
Encloses enzymes essential for metabolism (e.g., pyruvate dehydrogenase, citric acid cycle enzymes).
Contains mitochondrial genome, ribosomes, and tRNAs.
Components of the Electron Transport Chain
NADH:
Generated in the matrix by specific dehydrogenase reactions.
Transfers 2 electrons as a hydride (NAD+ + H+ + 2e- → NADH).
Flavoproteins:
Contain FAD or FMN.
Accept/donate electrons either one at a time or two at a time.
Typical standard reduction potential: ~0 V.
Coenzyme Q (Ubiquinone):
Soluble electron carrier in the lipid bilayer.
Able to accept/donate one or two electrons.
Cytochromes:
Contain heme groups for electron transfer.
Types include cytochromes b, c, and a/a3.
Distinct absorption spectra.
Iron-Sulfur Proteins:
Participate in single electron transfers with Fe2+ and Fe3+ states.
Characteristics include various clusters like FeS, Fe2S2, Fe3S4, and Fe4S4.
Copper Proteins:
Involved in one-electron transfers with Cu+ and Cu2+ states.
Overview of the Electron Transport Chain
Electrons move through the chain from donors to oxygen as the final acceptor.
Organized into 4 complexes (I-IV):
Complex I:
NADH dehydrogenase (NADH-Coenzyme Q reductase). Links glycolysis, citric acid cycle, and fatty acid oxidation to electron transport.
Complex II:
Succinate dehydrogenase, linking the citric acid cycle to electron transport.
Complex III:
Coenzyme Q reductase.
Complex IV:
Cytochrome c oxidase.
Functional Dynamics of Complexes
Complex I:
Transfers electrons from NADH to CoQ, generating a proton gradient.
Contains FMN and iron-sulfur clusters for electron transfer.
Complex II:
Catalyzes the conversion of succinate to fumarate while transferring electrons to CoQ.
Composed of four subunits, with covalently bound FAD.
Does not drive proton transport, resulting in lower ATP yield (1.5 ATP per FADH2 vs 2.5 ATP per NADH).
Advanced Cytochrome and Q-cycle in Complex III
The Q-cycle involves a series of electron transfers facilitated by CoQH2.
First step releases protons into the intermembrane space and generates semiquinone.
Further interactions ensure efficient electron transfer to cytochrome C, contributing to ATP synthesis.
Complex IV Functionality
Also known as cytochrome c oxidase; completes the reduction of oxygen.
Accepts electrons from cytochrome C to form water.
Involves a series of electron transfers and associated proton movements, supporting the final step in ATP synthesis.