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Oxidation of Са2+-Binding Domain of NADPH Oxidase 5 (NOX5): Toward Understanding the Mechanism of Inactivation of

Irina Yu Petrushanko1, Vladimir M Lobachev1, Alexey S Kononikhin2

  • 1Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov Street 32, 119991 Moscow, Russia.

Plos One
|July 9, 2016
PubMed

Insights

Oxidation of the NOX5 protein

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Biology

Background:

  • The NOX5 protein is a key producer of reactive oxygen species (ROS), crucial for cell regulation.
  • Tight regulation of NOX5 is essential for maintaining cellular homeostasis.
  • NOX5 possesses a unique calcium-binding domain, enabling direct activation by calcium ions.

Purpose of the Study:

  • To investigate the mechanisms that regulate NOX5 activity and prevent excessive ROS production.
  • To explore the impact of oxidation on the NOX5 protein's structure and function.

Main Methods:

  • Calorimetric methods were employed to assess protein stability and interactions.
  • Circular dichroism spectroscopy was used to analyze changes in protein secondary and tertiary structure.

Main Results:

  • Oxidation of cysteine and methionine residues in NOX5 was observed.
  • This oxidation led to reduced binding affinity for calcium ions.
  • Perturbations in both the secondary and tertiary structures of the NOX5 protein were detected.

Conclusions:

  • Oxidation of the calcium-binding domain in NOX5 appears to inactivate the protein.
  • This oxidative inactivation may serve as a protective mechanism against oxidative stress.
  • Understanding these regulatory mechanisms is vital for cellular health and disease research.

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