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

Item Type:Article
Title:3,5-Diiodothyronine binds to subunit Va of cytochrome-c oxidase and abolishes the allosteric inhibition of respiration by ATP
Creators Name:Arnold, S. and Goglia, F. and Kadenbach, B.
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.
Keywords:Cytochrome-C Oxidase, 3,5-Diiodothyronine, ATP/ADP Ratio, Subunit Va, Short-Term Action of Thyroid Hormones, Animals, Cattle
Source:European Journal of Biochemistry
ISSN:0014-2956
Publisher:Blackwell Publishing (U.K.)
Volume:252
Number:2
Page Range:325-330
Date:1 March 1998
Official Publication:https://doi.org/10.1046/j.1432-1327.1998.2520325.x
PubMed:View item in PubMed

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