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Related Experiment Videos

Coenzyme Q is an obligatory cofactor for uncoupling protein function.

K S Echtay1, E Winkler, M Klingenberg

  • 1Institute of Physiological Chemistry, University of Munich, Germany.

Nature
|December 16, 2000
PubMed
Summary

Coenzyme Q (ubiquinone) is identified as a crucial cofactor for Uncoupling Protein 1 (UCP1). This discovery clarifies UCP1

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Area of Science:

  • Mitochondrial physiology and bioenergetics
  • Molecular mechanisms of cellular respiration
  • Protein-cofactor interactions in energy metabolism

Background:

  • Uncoupling proteins (UCPs) dissipate mitochondrial gradients, producing heat instead of ATP.
  • UCP1's function and regulation by fatty acids, nucleotides, and pH remain debated.
  • Recombinant UCP1 in inclusion bodies lacked fatty-acid-dependent proton transport activity.

Purpose of the Study:

  • To identify a native cofactor essential for UCP1's proton transport activity.
  • To elucidate the role of coenzyme Q in UCP1-mediated proton transport.

Main Methods:

  • Reconstitution of UCP1 from inclusion bodies.
  • Assay of fatty-acid-dependent proton transport in reconstituted UCP1.
  • Investigation of coenzyme Q (CoQ10) and purine nucleotide effects on UCP1 activity.
  • Correlation of native UCP1 activity with endogenous coenzyme Q levels.

Main Results:

  • Coenzyme Q10 (CoQ10) addition restored fatty-acid-dependent proton transport in reconstituted UCP1.
  • Proton transport activity was sensitive to purine nucleotides and activated by oxidized CoQ.
  • Native UCP1 proton transport correlated with endogenous coenzyme Q content.

Conclusions:

  • Coenzyme Q (ubiquinone) is identified as a critical cofactor for UCP1.
  • This cofactor is essential for UCP1's fatty-acid-activated proton transport.
  • The findings resolve controversies regarding UCP1 regulation and function.

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