Interaction of diiodothyronines with isolated cytochrome c oxidase
Abstract
Diiodothyronines (3,3′‐T 2 and 3,5‐T 2) stimulate the activity of isolated cytochrome c oxidase (COX) from bovine heart mitochondria. Maximal stimulation of activity (about 50%) is obtained with 3,3′‐T 2 at pH 6.4 and with 3,5‐T 2 at pH 7.4. In contrast, 3,5,3′‐triiodothyronine (T 3) 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.
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3,5-T2 affects the activity of enzymes involved in energy metabolism.
“and affects the activity of enzymes involved in energy metabolism, including α-glycerophosphate dehydrogenase (Lombardi et al. 2000), cytochrome oxidase (Lanni et al. 1992, 1993, Goglia et al. 1994, Arnold et al. 1998), malate dehydrogenase (Ball et al. 1997, Lombardi et al. 2000), glucose-6-phosphate dehydrogenase (Lombardi et al. 2000), and F0F1-ATP synthase (Mangiullo et al. 2010).”
From Administration of 3,5-diiodothyronine (3,5-T2) causes central hypothyroidism and stimulates thyroid-sensitive tissues (2014) · cites this paper as Goglia et al. 1994
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Binding Characteristics of Thyroid Hormone Distributor Proteins to Thyroid Hormone Metabolites
Jongejan, R. M. S., Meima, M. E., Visser, W. E., Korevaar, T. I. M., van den Berg, S. A. A., Peeters, R. P., & de Rijke, Y. B. (2022) · Thyroid® · doi:10.1089/thy.2021.0588 · Cited by 20 · see citing works
- Authors
- Goglia, F., Lanni, A., Barth, J., & Kadenbach, B.
- Affiliations
- University of Naples Federico II (IT)
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1994-06-13
- Volume
- 346
- Issue
- 2-3
- Pages
- 295-298
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W1973608509
- Cited by
- 71
- References
- 0
- Citations by year
- 2025: 1 · 2024: 1 · 2023: 1 · 2022: 3 · 2020: 1 · 2019: 2 · 2018: 3 · 2017: 3 · 2016: 2 · 2015: 3 · 2014: 2 · 2013: 6 · 2012: 2
- FWCI
- 1.68
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Archivio Istituzionale della Ricerca - Università degli Studi della Campania "Luigi Vanvitelli" (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Thyroid Disorders and Treatments
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Keywords
- diiodothyronine, triiodothyronine, cytochrome c oxidase, thyroid hormones, allosteric regulation, mitochondrial respiration, enzyme activation, conformational change, heart mitochondria, pH dependence
- MeSH terms
- Animals, Cattle, Electron Transport Complex IV, Diiodothyronines, Hydrogen-Ion Concentration, Mitochondria, Heart, Oxygen Consumption, Protein Conformation, Spectrophotometry, Triiodothyronine
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