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Related Concept Videos

Electron Transport Chain: Complex I and II01:46

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The final stage of cellular respiration is oxidative phosphorylation that consists of two steps: the electron transport chain and chemiosmosis. The electron transport chain is a set of proteins found in the inner mitochondrial membrane in eukaryotic cells. Its primary function is to establish a proton gradient that can be used during chemiosmosis to produce ATP and generate electron carriers, such as NAD+ and FAD, that are used in glycolysis and the citric acid cycle.
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During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
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The electron transport chain (ETC) is a crucial metabolic pathway that facilitates energy conversion in prokaryotic and eukaryotic cells. In eukaryotes, the ETC comprises four membrane-associated protein complexes in the inner mitochondrial membrane. In prokaryotes, the ETC in the plasma membrane can vary in composition, with fewer or different complexes depending on the organism and environmental conditions. These complexes transfer electrons from electron donors, such as NADH and FADH2, to...
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The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...
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Electron-transfer chain in respiratory complex I.

Daniel R Martin1, Dmitry V Matyushov2

  • 1Department of Physics and School of Molecular Sciences, Arizona State University, PO Box 871504, Tempe, AZ, 85287-1504, USA.

Scientific Reports
|July 16, 2017
PubMed
Summary
This summary is machine-generated.

Complex I, crucial for cellular respiration, uses iron-sulfur clusters and water interactions to efficiently transfer electrons. This mechanism lowers energy barriers, ensuring robust energy conversion for proton pumping.

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Area of Science:

  • Biochemistry
  • Bioenergetics
  • Protein Dynamics

Background:

  • Complex I is a key enzyme in the respiratory electron-transfer chain, generating proton gradients for ATP synthesis.
  • It contains an electron-transfer chain of iron-sulfur cofactors within its peripheral subunit.
  • Protein hydration and water-cofactor interactions are critical for enzyme function.

Purpose of the Study:

  • To elucidate the mechanisms by which Complex I achieves efficient electron transfer.
  • To investigate the role of protein-water interface and iron-sulfur clusters in lowering activation barriers.
  • To understand how quantum effects and protein dynamics contribute to enzyme efficiency.

Main Methods:

  • Analysis of electron transfer pathways and cofactor interactions.
  • Investigating the influence of protein-water interface dynamics on electron transfer rates.
  • Theoretical modeling incorporating electrostatic noise and quantum states.

Main Results:

  • The protein-water interface generates electrostatic noise, while iron-sulfur clusters possess high quantum state density due to spin interactions.
  • This combination significantly lowers electron transfer activation barriers below Marcus theory predictions.
  • Water actively participates in electron transport by electrowetting cofactors.

Conclusions:

  • Iron-sulfur clusters merge protein-water fluctuations with quantum multiplicity for low activation barriers and robust electron transfer.
  • Water's role in electrowetting cofactors is vital for electron transport energetics.
  • Nonergodic sampling of the protein landscape contributes to the high functional efficiency of redox enzymes like Complex I.