Interaction of diiodothyronines with isolated cytochromec oxidase
Open Access
- 13 June 1994
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 346 (2-3) , 295-298
- https://doi.org/10.1016/0014-5793(94)00476-5
Abstract
Diiodothyronines (3,3′‐T2 and 3,5‐T2) stimulate the activity of isolated cytochromec oxidase (COX) from bovine heart mitochondria. Maximal stimulation of activity (about 50%) is obtained with 3,3′‐T2 at pH 6.4 and with 3,5‐T2 at pH 7.4. In contrast, 3,5,3′‐triiodothyronine (T3) exhibited no or little stimulation of COX activity. Binding of the hormones to COX leads to conformational changes as shown by modified visible spectra of the oxidized enzyme. It is suggested that ‘short‐term’ effects of thyroid hormones on mitochondrial respiration are at least partly due to the allosteric interaction of diiodothyronines with the COX complex.Keywords
This publication has 27 references indexed in Scilit:
- Rapid stimulation in vitro of rat liver cytochrome oxidase activity by 3,5-diiodo-l-thyronine and by 3,3′-diiodo-l-thyronineMolecular and Cellular Endocrinology, 1994
- Tissue-specific regulation of cytochrome c oxidase efficiency by nucleotidesBiochemistry, 1993
- Effect of 3,3′-diiodothyronine and 3,5-diiodothyronine on rat liver oxidative capacityMolecular and Cellular Endocrinology, 1992
- Thyroid hormone uptake into the cell and its subsequent localisation to the mitochondriaFEBS Letters, 1987
- CONTROL OF ELECTRON FLUX THROUGH THE RESPIRATORY CHAIN IN MITOCHONDRIA AND CELLSBiological Reviews, 1987
- Localization of 3,5,3′-L-triiodothyronine receptor in rat kidney mitochondrial membranesBiochemical and Biophysical Research Communications, 1982
- Rapid and direct stimulation of hepatic gluconeogenesis by L-triiodothyronine (T3) in the isolated-perfused rat liverLife Sciences, 1980
- IN BRIEFInPharma, 1980
- Reading Delacroix's "Journal"October, 1980
- Thyroid Hormone Action: The Mitochondrial PathwayScience, 1977