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Related Experiment Videos

Nitric oxide and mitochondrial complex IV.

Paolo Sarti1, Marzia Arese, Antonella Bacchi

  • 1Department of Biochemical Sciences, University of Rome La Sapienza 1-00185 Rome, Italy. paolo.sarti@uniroma1.it

IUBMB Life
|January 9, 2004
PubMed
Summary

Nitric oxide (NO) rapidly inhibits cytochrome c oxidase through two mechanisms. The cell

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Area of Science:

  • Biochemistry
  • Cellular Respiration
  • Enzyme Kinetics

Background:

  • Nitric oxide (NO) is a signaling molecule with complex interactions in cellular respiration.
  • Cytochrome c oxidase is a key enzyme in the electron transport chain, sensitive to NO.
  • Understanding NO's effects on this enzyme is crucial for pathophysiology.

Purpose of the Study:

  • To elucidate the reaction mechanisms between nitric oxide and cytochrome c oxidase.
  • To investigate the reversibility and kinetics of NO-induced inhibition.
  • To determine factors influencing the NO-cytochrome c oxidase interaction.

Main Methods:

  • Enzyme kinetics studies with purified cytochrome c oxidase.
  • Oxygraphic measurements in isolated mitochondria (state 4 and state 3).

Related Experiment Videos

  • Experiments using cultured human SY5Y neuroblastoma cells.

    • Main Results:

    • Two NO-enzyme adducts identified: nitrosyl and nitrite derivatives.
    • Nitrite adduct formation leads to faster recovery of enzyme activity.
    • Reduced cytochrome c concentration is a key factor determining the NO reaction pathway.

    Conclusions:

    • NO inhibition of cytochrome c oxidase is reversible, with kinetics dependent on the reaction mechanism.
    • The enzyme can either be inhibited or facilitate NO degradation depending on the pathway.
    • Cellular redox state significantly influences the interaction between NO and cytochrome c oxidase.