3,5-Diiodothyronine binds to subunit Va of cytochrome-c oxidase and abolishes the allosteric inhibition of respiration by ATP

Eur J Biochem. 1998 Mar 1;252(2):325-30. doi: 10.1046/j.1432-1327.1998.2520325.x.

Abstract

The short-term effects of thyroid hormones, which do not occur via gene expression, were postulated to be based on interaction of diiodothyronines with mitochondria. We demonstrate specific binding of labelled 3,5-diiodothyronine to subunit Va of cytochrome-c oxidase from bovine heart. 3,5-Diiodothyronine, and to a small extent triiodothyronine, but not thyroxine and thyronine, abolish the allosteric inhibition of ascorbate respiration of reconstituted cytochrome c oxidase by ATP [Arnold, S. & Kadenbach, B. (1997) Eur. J. Biochem. 249, 350-354]. This abolition of ATP-inhibition by 3,5-diiodothyronine is completely prevented by a monoclonal antibody to subunit Va. The results explain at the molecular level the short-term action of thyroid hormones on basal metabolic rate.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / pharmacology*
  • Allosteric Regulation / drug effects
  • Allosteric Regulation / physiology
  • Allosteric Site / physiology
  • Animals
  • Ascorbic Acid / metabolism
  • Cattle
  • Cell Respiration / drug effects
  • Electron Transport Complex IV / metabolism*
  • Iodine Radioisotopes / metabolism
  • Mitochondria, Heart / drug effects
  • Mitochondria, Heart / enzymology*
  • Models, Molecular
  • Protein Binding / physiology
  • Triiodothyronine / pharmacology*

Substances

  • Iodine Radioisotopes
  • Triiodothyronine
  • Adenosine Triphosphate
  • Electron Transport Complex IV
  • Ascorbic Acid