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Nitric oxide interacts with mitochondrial complex III producing antimycin-like effects.

Darío E Iglesias1, Silvina S Bombicino1, Laura B Valdez1

  • 1Institute of Biochemistry and Molecular Medicine, Physical Chemistry Division, School of Pharmacy and Biochemistry, University of Buenos Aires (IBIMOL, UBA-CONICET). Junín 956, C1113AAD Buenos Aires, Argentina.

Free Radical Biology & Medicine
|October 13, 2015
PubMed
Summary

Nitric oxide (NO) inhibits mitochondrial complex III activity by interacting with the ubiquinone-cytochrome b region. This leads to reduced electron transfer and increased mitochondrial reactive oxygen species production.

Keywords:
Cytochrome bc(1) complexElectron paramagnetic resonance (EPR)Hydrogen peroxideNitric oxideS-nitrosoglutathione (GSNO)Spermine-NONOate (SPER-NO)Superoxide anionUbiquinone-cytochrome b areaUbisemiquinone

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Area of Science:

  • Biochemistry
  • Mitochondrial Physiology
  • Cellular Respiration

Background:

  • Mitochondrial respiratory chain complexes are crucial for cellular energy production.
  • Nitric oxide (NO) is a signaling molecule with known effects on cellular processes, including mitochondrial function.
  • The precise interaction of NO with specific components of the respiratory chain, particularly complex III, requires further elucidation.

Purpose of the Study:

  • To investigate the effect of nitric oxide (NO) on the mitochondrial respiratory chain, specifically focusing on the ubiquinone-cytochrome b region.
  • To determine the impact of NO on complex III activity and its downstream consequences on reactive oxygen species (ROS) production.

Main Methods:

  • Utilized submitochondrial particles (SMP) from bovine heart.
  • Employed S-nitrosoglutathione (GSNO) and S-nitroso-N-acetylpenicillamine (SPER-NO) as sources of NO.
  • Assessed enzyme activities (succinate-cytochrome c reductase, succinate-Q reductase), cytochrome b562 reduction, and reactive oxygen species (O2(•-) and H2O2) production.
  • Employed Electron Paramagnetic Resonance (EPR) spectroscopy to detect semiquinone radicals.

Main Results:

  • NO significantly inhibited succinate-cytochrome c reductase (complex II-III) activity, but not succinate-Q reductase (complex II) activity, indicating an effect on complex III.
  • Endogenous NO, generated from L-arginine and mtNOS cofactors, also decreased complex II-III activity.
  • GSNO treatment reduced cytochrome b562 and increased mitochondrial O2(•-) and H2O2 production.
  • EPR analysis revealed increased semiquinone signals upon NO exposure, similar to antimycin, suggesting an interaction with the ubiquinone-cytochrome b region.

Conclusions:

  • Nitric oxide (NO) directly interacts with the ubiquinone-cytochrome b region of the mitochondrial respiratory chain.
  • This interaction leads to antimycin-like effects, including inhibition of electron transfer and cytochrome b oxidation.
  • NO-induced alterations in the ubiquinone pool enhance mitochondrial superoxide and hydrogen peroxide production.