Abstract
We show that tetraphenylphosphonium inhibits oxidation of palmitoylcarnitine, pyruvate, malate, 2-oxoglutarate and glutamate in heart mitochondria in the range of concentration (1–5 µM) commonly used for the determination of mitochondrial membrane potential. The inhibition of 2-oxoglutarate (but not other substrate) oxidation by tetraphenylphosphonium is dependent on the concentration of 2-oxoglutarate and on extramitochondrial free calcium, and the kinetic plots are consistent with a mixed type of inhibition. Our results indicate that tetraphenylphosphonium interacts with enzymes, specifically involved in the oxidation of 2-oxoglutarate, most possibly, 2-oxoglutarate dehydrogenase. (Mol Cell Biochem 174: 67-70, 1997)
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Abbreviations
- TPP+ :
-
tetraphenylphosphonium
- TPMP+ :
-
triphenylmethylphosphonium
References
Grinius LL, Jasaitis AA, Kadziauskas JP, Liberman EA, Skulachev VP, Topali VP, Tsofina FM, Vladimirova MA: Conversion of biomembrane-produced energy into electric form. I. Submitochondrial particles. Biochim Biophys Acta 216: 1–12, 1970
Bakeeva LE, Grinius LL, Jasaitis AA, Kuliene VV, Levitsky DO, Liberman EA, Severina II, Skulachev VP: Conversion of biomembrane-produced energy into electric form. II. Intact Mitochondria. Biochim Biophys Acta 216: 13–21, 1970
Kashket ER: The protonmotive force in bacteria: a critical assessment of methods. Ann Rev Microbiol 39: 210–242, 1985
Brand MD: Measurement of mitochondrial protonmotive force. In: GC Brown, CE Cooper (eds). Bioenergetics — A Practical Approach. Oxford University Press, Oxford, New York, Tokyo, 1994, pp 39–62
Kamo N, Muragatsu M, Hongoh R, Kotabake YJ: Membrane potential of mitochondria measured with an electrode sensitive to tetraphenyl phosphonium and relationship between electrochemical potential and phosphorylation potential in steady state. J Membr Biol 49:105–121, 1979
Wingrove DE, Gunter TE: Kinetics of mitochondrial calcium transport. II. A kinetic description of the sodium-dependent calcium efflux mechanism in liver mitochondria and inhibition by ruthenium red and by tetraphenylphosphonium. J Biol Chem 261: 15166–15171, 1986.
Mildaziene V, Baniene R, Nauciene Z, Bakker BM, Brown GC, Westerhoff HV, Kholodenko BN: Calcium indirectly increases the control exerted by the adenine nucleotide translocator over 2-oxoglutarate oxidation in rat heart mitochondria. Arch Biochem Biophys 324:130–134, 1995
Fabiato A, Fabiato FJ: Calculator programs for multiple metals and ligands. J Physiol (Paris) 75: 463–505, 1979
Demura M, Kamo N, Kobatake Y: Mitochondrial membrane potential estimated with the correction of probe binding. Biochim Biophys Acta 894: 355–364, 1987
McCormack JG, Denton RM: The effects of calcium ions and adenine nucleotides on the activity of pig heart 2-oxoglutarate dehydrogenase complex. Biochem J 180: 533–544, 1979
Panov AV, Scaduto RC: Influence of calcium on NADH and succinate oxidation by rat heart submitochondrial particles. Arch Biochem Biophys 316:815–820, 1995
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1997 Springer Science+Business Media Dordrecht
About this chapter
Cite this chapter
Mildaziene, V., Baniene, R., Marcinkeviciute, A., Nauciene, Z., Kalvenas, A., Zimkus, A. (1997). Tetraphenylphosphonium inhibits oxidation of physiological substrates in heart mitochondria. In: Gellerich, F.N., Zierz, S. (eds) Detection of Mitochondrial Diseases. Developments in Molecular and Cellular Biochemistry, vol 21. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-6111-8_10
Download citation
DOI: https://doi.org/10.1007/978-1-4615-6111-8_10
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-7800-6
Online ISBN: 978-1-4615-6111-8
eBook Packages: Springer Book Archive