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Related Experiment Videos

A role for copper in biological time-keeping.

Ziying Jiang1, Dorothy M Morré, D James Morré

  • 1Department of Medicinal Chemistry and Molecular Pharmacology, Hansen Life Sciences Research Building, Purdue University, 201 S. University Street, West Lafayette, IN 47907-2064, USA.

Journal of Inorganic Biochemistry
|October 10, 2006
PubMed
Summary

Copper is essential for the 24-minute oscillation cycle of ECTO-NOX proteins, which regulate cell growth. Released copper alone can also catalyze and oscillate NADH oxidation, suggesting copper

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Physiology

Background:

  • ECTO-NOX proteins are cell surface enzymes involved in growth regulation.
  • These proteins catalyze NADH/hydroquinone oxidation and protein disulfide-thiol interchange.
  • A specific protein, CNOX, exhibits a 24-minute oscillation cycle in its activity.

Purpose of the Study:

  • To investigate the role of bound copper (Cu(II)) in the 24-minute oscillation cycle of CNOX.
  • To determine if copper itself can catalyze NADH oxidation and exhibit oscillatory behavior.

Main Methods:

  • Soybean CNOX preparations were unfolded and refolded in the presence and absence of a copper chelator (bathocuproine).
  • Activity was measured by monitoring NADH or hydroquinone oxidation.

Related Experiment Videos

  • Solvated Cu(II) salts were tested for their ability to catalyze NADH oxidation and their oscillatory patterns were analyzed.

    • Main Results:

    • Bound Cu(II) is required for CNOX activity and its 24-minute oscillation cycle.
    • Refolding CNOX without copper abolished activity, which was restored upon copper addition.
    • Released copper alone catalyzed NADH oxidation, exhibiting an oscillatory pattern with a 24-minute period, independent of temperature and pH.

    Conclusions:

    • Bound copper is crucial for maintaining the structural changes underlying CNOX's periodic activity.
    • Copper ions themselves possess catalytic and oscillatory properties relevant to the ECTO-NOX protein family.
    • These findings highlight the critical role of copper in the time-keeping mechanism of CNOX and potentially other ECTO-NOX proteins.