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. 1978 Mar 15;170(3):503–510. doi: 10.1042/bj1700503

Citreoviridin, a specific inhibitor of the mitochondiral adenosine triphosphatase.

P E Linnett, A D Mitchell, M D Osselton, L J Mulheirn, R B Beechey
PMCID: PMC1183925  PMID: 148274

Abstract

1. Citreoviridin was a potent inhibitor of the soluble mitochondrial ATPase (adenosine triphosphatase) similar to the closely related aurovertins B and D. 2. Citreoviridin inhibited the following mitochondrial energy-linked reactions also: ADP-stimulated respiration in whole mitochondria from ox heart and rat liver; ATP-driven reduction of NAD+ by succinate; ATP-driven NAD transhydrogenase and ATPase from ox heart submitochondrial particles. 3. The dissociation constant (KD) calculated by a simple law-of-mass-action treatment for the citreoviridin--ATPase complex was 0.5--4.2micron for ox-heart mitochondrial preparations and 0.15micron for rat liver mitochondria. 4. Monoacetylation of citreoviridin decreased its inhibitory potency (KD=2--25micron, ox heart; KD=0.7micron, rat liver). Diacetylation greatly decreased the inhibitory potency (KD=60--215micron, ox heart). 5. Hydrogenation of citreoviridin monoacetate diminished its inhibitory potency considerably. 6. No significant enhancement of fluorescence was observed when citreoviridin interacted with the mitochondrial ATPase.

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Selected References

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  1. Beechey R. B., Hubbard S. A., Linnett P. E., Mitchell A. D., Munn E. A. A simple and rapid method for the preparation of adenosine triphosphatase from submitochondrial particles. Biochem J. 1975 Jun;148(3):533–537. doi: 10.1042/bj1480533. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bertina R. M., Schrier P. I., Slater E. C. The binding of aurovertin to mitochondria, and its effect on mitochondrial respiration. Biochim Biophys Acta. 1973 Jun 28;305(3):503–518. doi: 10.1016/0005-2728(73)90072-8. [DOI] [PubMed] [Google Scholar]
  3. CHANCE B., WILLIAMS G. R. Respiratory enzymes in oxidative phosphorylation. III. The steady state. J Biol Chem. 1955 Nov;217(1):409–427. [PubMed] [Google Scholar]
  4. Chang T. M., Penefsky H. S. Energy-dependent enhancement of aurovertin fluorescence. An indicator of conformational changes in beef heart mitochondrial adenosine triphosphatase. J Biol Chem. 1974 Feb 25;249(4):1090–1098. [PubMed] [Google Scholar]
  5. Chang T., Penefsky H. S. Aurovertin, a fluorescent probe of conformational change in beef heart mitochondrial adenosine triphosphatase. J Biol Chem. 1973 Apr 25;248(8):2746–2754. [PubMed] [Google Scholar]
  6. Chappell J. B. The oxidation of citrate, isocitrate and cis-aconitate by isolated mitochondria. Biochem J. 1964 Feb;90(2):225–237. doi: 10.1042/bj0900225. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Ebel R. E., Lardy H. A. Influence of aurovertin on mitochondrial ATPase activity. J Biol Chem. 1975 Jul 10;250(13):4992–4995. [PubMed] [Google Scholar]
  8. Kagawa Y., Racker E. Partial resolution of the enzymes catalyzing oxidative phosphorylation. 8. Properties of a factor conferring oligomycin sensitivity on mitochondrial adenosine triphosphatase. J Biol Chem. 1966 May 25;241(10):2461–2466. [PubMed] [Google Scholar]
  9. LARDY H. A., CONNELLY J. L., JOHNSON D. ANTIBIOTIC STUDIES. II. INHIBITION OF PHOSPHORYL TRANSFER IN MITOCHONDRIA BY OLIGOMYCIN AND AUROVERTIN. Biochemistry. 1964 Dec;3:1961–1968. doi: 10.1021/bi00900a030. [DOI] [PubMed] [Google Scholar]
  10. Lambeth D. O., Lardy H. A. Purification and properties of rat-liver-mitochondrial adenosine triphosphatase. Eur J Biochem. 1971 Oct 14;22(3):355–363. doi: 10.1111/j.1432-1033.1971.tb01552.x. [DOI] [PubMed] [Google Scholar]
  11. Layton D., Azzi A., Graziotti P. The use of the fluorescent probe aurovertin, to monitor energy linked conformational changes in mitochondrial ATPases. FEBS Lett. 1973 Oct 1;36(1):87–92. doi: 10.1016/0014-5793(73)80343-6. [DOI] [PubMed] [Google Scholar]
  12. Lee C., Ernster L. Studies of the energy-transfer system of submitochondrial particles. 2. Effects of oligomycin and aurovertin. Eur J Biochem. 1968 Feb;3(4):391–400. doi: 10.1111/j.1432-1033.1967.tb19542.x. [DOI] [PubMed] [Google Scholar]
  13. Lenaz G. Effect of aurovertin on energy-linked processes related to oxidative phosphorylation. Biochem Biophys Res Commun. 1965 Oct 26;21(2):170–175. doi: 10.1016/0006-291x(65)90104-x. [DOI] [PubMed] [Google Scholar]
  14. Linnett P. E., Mitchell A. D., Beechey R. B., Baum H. A reiteration of the equation derived by Easson & Stedman (1936) and its application to the inhibition of mitochondrial energy-linked functions by the aurovertins [proceedings]. Biochem Soc Trans. 1977;5(5):1510–1511. doi: 10.1042/bst0051510. [DOI] [PubMed] [Google Scholar]
  15. PULLMAN M. E., PENEFSKY H. S., DATTA A., RACKER E. Partial resolution of the enzymes catalyzing oxidative phosphorylation. I. Purification and properties of soluble dinitrophenol-stimulated adenosine triphosphatase. J Biol Chem. 1960 Nov;235:3322–3329. [PubMed] [Google Scholar]
  16. Roberton A. M., Beechey R. B., Holloway C. T., Knight I. G. The effect of aurovertin on a soluble mitochondrial adenosine triphosphatase. Biochem J. 1967 Sep;104(3):54C–55C. doi: 10.1042/bj1040054c. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Roberton A. M., Holloway C. T., Knight I. G., Beechey R. B. A comparison of the effects of NN'-dicyclohexylcarbodi-imide, oligomycin A and aurovertin on enrgy-linked reactions in mitochondria and submitochondrial particles. Biochem J. 1968 Jul;108(3):445–456. doi: 10.1042/bj1080445. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. van de Stadt R. J., van Dam K. Binding of aurovertin to phosphorylating submitochondrial particles. Biochim Biophys Acta. 1974 May 22;347(2):253–263. doi: 10.1016/0005-2728(74)90049-8. [DOI] [PubMed] [Google Scholar]
  19. van de Stadt R. J., van Dam K., Slater E. C. Interaction of aurovertin with submitochondrial particles, deficient in ATPase inhibitor. Biochim Biophys Acta. 1974 May 22;347(2):224–239. doi: 10.1016/0005-2728(74)90047-4. [DOI] [PubMed] [Google Scholar]

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