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Pyruvate Oxidation01:15

Pyruvate Oxidation

After glycolysis, the charged pyruvate molecules enter the mitochondria via active transport and undergo three enzymatic reactions. These reactions ensure that pyruvate can enter the next metabolic pathway so that energy stored in the pyruvate molecules can be harnessed by the cells.
First, the enzyme pyruvate dehydrogenase removes the carboxyl group from pyruvate and releases it as carbon dioxide. The stripped molecule is then oxidized and releases electrons, which are then picked up by NAD+...
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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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Updated: May 27, 2026

Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases
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Published on: February 24, 2018

Nitrogen dioxide oxidizes mitochondrial cytochrome c.

Rebecca S Silkstone1, Maria G Mason, Peter Nicholls

  • 1Department of Biological Sciences, University of Essex, Colchester, Essex, UK.

Free Radical Biology & Medicine
|November 22, 2011
PubMed
Summary
This summary is machine-generated.

Nitric oxide (NO) does not directly oxidize mitochondrial cytochrome c. Instead, nitrogen dioxide (NO2•), formed during NO

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Oxygen-Independent Assays to Measure Mitochondrial Function in Mammals

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Area of Science:

  • Biochemistry
  • Cellular Respiration
  • Oxidative Stress

Background:

  • Previous studies suggested nitric oxide (NO) directly oxidizes mitochondrial cytochrome c.
  • Re-evaluation of redox potentials indicated this reaction is thermodynamically unfavorable.

Purpose of the Study:

  • To investigate the mechanism of nitric oxide-mediated cytochrome c oxidation.
  • To identify the reactive species responsible for cytochrome c oxidation by NO.

Main Methods:

  • Studying the oxygen-concentration dependence of NO-induced cytochrome c oxidation.
  • Employing kinetic modeling of NO autoxidation.
  • Utilizing scavengers like urate and ferrocyanide to probe the reaction mechanism.

Main Results:

  • Cytochrome c oxidation by NO is oxygen-dependent and non-stoichiometric.
  • The primary oxidant is identified as nitrogen dioxide (NO2•), a product of NO aerobic decay.
  • A kinetic model accurately predicted cytochrome c oxidation rates with NO2•.
  • Scavengers confirmed the role of NO2• by altering oxidation extents.

Conclusions:

  • The direct oxidation of cytochrome c by NO is unlikely.
  • Nitrogen dioxide (NO2•) is the principal species mediating cytochrome c oxidation in aerobic conditions.
  • The findings refute previous hypotheses involving nitroxyl ions or peroxynitrite in this reaction.