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Electron Transport Chain Components01:29

Electron Transport Chain Components

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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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Electron Transport Chain: Complex III and IV01:43

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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 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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Chemiosmosis and ATP Synthesis01:22

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The electron transport chain is a critical component of cellular respiration, occurring in the inner mitochondrial membrane. It facilitates the transfer of high-energy electrons from reduced cofactors NADH and FADH₂ to molecular oxygen, the final electron acceptor. This transfer of electrons through a series of protein complexes is tightly coupled to the translocation of protons across the membrane, generating a proton gradient essential for ATP synthesis.Electron Flow and Proton...
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The light reactions of photosynthesis assume a linear flow of electrons from water to NADP+. During this process, light energy drives the splitting of water molecules to produce oxygen. However, oxidation of water molecules is a thermodynamically unfavorable reaction and requires a strong oxidizing agent. This is accomplished by the first product of light reactions: oxidized P680 (or P680+), the most powerful oxidizing agent known in biology. The oxidized P680 that acquires an electron from the...
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The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
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NOX Transmembrane Electron Transfer Is Governed by a Subtly Balanced, Self-Adjusting Charge Distribution.

Baptiste Etcheverry1, Marc Baaden2, Aurélien de la Lande1

  • 1Institut de Chimie Physique, Université Paris Saclay, CNRS (UMR 8000), 15 avenue Jean Perrin, Orsay 91405, France.

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This study reveals how membrane charge and protein sequence influence electron transfer in NADPH oxidases (NOX). Despite modifications, the overall free energy remains favorable for electron transfer, crucial for reactive oxygen species production.

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Area of Science:

  • Biochemistry
  • Biophysics
  • Molecular Biology

Background:

  • NADPH oxidases (NOX) are transmembrane enzymes generating reactive oxygen species via electron transfer (ET).
  • These enzymes utilize flavin and heme cofactors for redox mediation across membranes.
  • Understanding the thermodynamics of inter-heme ET is key to NOX function.

Purpose of the Study:

  • To investigate the thermodynamics of electron transfer between hemes in the NOX5 transmembrane domain.
  • To compare these processes in human (hNOX5) and cyanobacterial (csNOX5) isoforms.
  • To elucidate the impact of membrane lipid charge and amino acid sequence on ET thermodynamics.

Main Methods:

  • Extensive molecular dynamics simulations were employed.
  • Linear response formalism was used to decompose free energy contributions.
  • Comparisons were made between hNOX5 and csNOX5 under varying membrane conditions.

Main Results:

  • Membrane charge density and NOX5 amino acid sequence significantly influence ET thermodynamics.
  • Compensatory effects among protein, membrane, and solvent components were observed.
  • Total free energy consistently favored electron transfer, despite individual component variations.

Conclusions:

  • The study provides the first insights into membrane charge density effects on inter-heme ET in NOX enzymes.
  • Molecular mechanisms governing ET catalysis in complex membrane environments are illuminated.
  • Findings are crucial for understanding reactive oxygen species generation and NOX enzyme function.