Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1984 May 1;219(3):1043–1047. doi: 10.1042/bj2191043

Measurement of the oxidation-reduction potentials for one-electron and two-electron reduction of electron-transfer flavoprotein from pig liver.

M Husain, M T Stankovich, B G Fox
PMCID: PMC1153579  PMID: 6743239

Abstract

Potentiometric titrations of pig liver electron-transfer flavoprotein (ETF) were performed at pH 7.5 and 4 degrees C, both in the reductive and oxidative directions. Reduction of ETF to the hydroquinone form required a total of two reducing equivalents/mol of ETF with the formation of sub-stoichiometric amounts of anionic semiquinone as an intermediate. The oxidation-reduction potentials for the two one-electron couples, oxidized ETF/ETF semiquinone and ETF semiquinone/fully reduced ETF, are +4 mV and -50 mV respectively. The overall midpoint potential for the two-electron couple (oxidized ETF/fully reduced ETF) is -23 mV.

Full text

PDF
1043

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Beckmann J. D., Frerman F. E., McKean M. C. Inhibition of general acyl CoA dehydrogenase by electron transfer flavoprotein semiquinone. Biochem Biophys Res Commun. 1981 Oct 30;102(4):1290–1294. doi: 10.1016/s0006-291x(81)80151-9. [DOI] [PubMed] [Google Scholar]
  2. CRANE F. L., BEINERT H. On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. II. The electron-transferring flavoprotein. J Biol Chem. 1956 Feb;218(2):717–731. [PubMed] [Google Scholar]
  3. CRANE F. L., MII S., HAUGE J. G., GREEN D. E., BEINERT H. On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. I. The general fatty acyl coenzyme A dehydrogenase. J Biol Chem. 1956 Feb;218(2):701–706. [PubMed] [Google Scholar]
  4. Choong Y. S., Massey V. Stabilization of lactate oxidase flavin anion radical by complex formation. J Biol Chem. 1980 Sep 25;255(18):8672–8677. [PubMed] [Google Scholar]
  5. FRISELL W. R., MACKENZIE C. G. Separation and purification of sarcosine dehydrogenase and dimethylglycine dehydrogenase. J Biol Chem. 1962 Jan;237:94–98. [PubMed] [Google Scholar]
  6. Gorelick R. J., Mizzer J. P., Thorpe C. Purification and properties of electron-transferring flavoprotein from pig kidney. Biochemistry. 1982 Dec 21;21(26):6936–6942. doi: 10.1021/bi00269a049. [DOI] [PubMed] [Google Scholar]
  7. HAUGE J. G., CRANE F. L., BEINERT H. On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. III. Palmityl coA dehydrogenase. J Biol Chem. 1956 Apr;219(2):727–733. [PubMed] [Google Scholar]
  8. Hall C. L., Kamin H. The purification and some properties of electron transfer flavoprotein and general fatty acyl coenzyme A dehydrogenase from pig liver mitochondria. J Biol Chem. 1975 May 10;250(9):3476–3486. [PubMed] [Google Scholar]
  9. Hall C. L., Lambeth J. D. Studies on electron transfer from general acyl-CoA dehydrogenase to electron transfer flavoprotein. J Biol Chem. 1980 Apr 25;255(8):3591–3595. [PubMed] [Google Scholar]
  10. Husain M., Steenkamp D. J. Electron transfer flavoprotein from pig liver mitochondria. A simple purification and re-evaluation of some of the molecular properties. Biochem J. 1983 Feb 1;209(2):541–545. doi: 10.1042/bj2090541. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Mayhew S. G., Massey V. Purification and characterization of flavodoxin from Peptostreptococcus elsdenii. J Biol Chem. 1969 Feb 10;244(3):794–802. [PubMed] [Google Scholar]
  12. McKean M. C., Beckmann J. D., Frerman F. E. Subunit structure of electron transfer flavoprotein. J Biol Chem. 1983 Feb 10;258(3):1866–1870. [PubMed] [Google Scholar]
  13. McKean M. C., Frerman F. E., Mielke D. M. General acyl-CoA dehydrogenase from pig liver. Kinetic and binding studies. J Biol Chem. 1979 Apr 25;254(8):2730–2735. [PubMed] [Google Scholar]
  14. Noda C., Rhead W. J., Tanaka K. Isovaleryl-CoA dehydrogenase: demonstration in rat liver mitochondria by ion exchange chromatography and isoelectric focusing. Proc Natl Acad Sci U S A. 1980 May;77(5):2646–2650. doi: 10.1073/pnas.77.5.2646. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. O'Reilly J. E. Oxidation-reduction potential of the ferro-ferricyanide system in buffer solutions. Biochim Biophys Acta. 1973 Apr 5;292(3):509–515. doi: 10.1016/0005-2728(73)90001-7. [DOI] [PubMed] [Google Scholar]
  16. Reinsch J. W., Feinberg B. A., McFarland J. T. Intermediates during the fatty acyl CoA dehydrogenase catalyzed reduction of electron transfer flavoprotein (ETF) by fatty acyl CoA esters. Biochem Biophys Res Commun. 1980 Jun 30;94(4):1409–1416. doi: 10.1016/0006-291x(80)90576-8. [DOI] [PubMed] [Google Scholar]
  17. Rhead W., Mantagos S., Tanaka K. Glutaric aciduria type II: in vitro studies on substrate oxidation, acyl-CoA dehydrogenases, and electron-transferring flavoprotein in cultured skin fibroblasts. Pediatr Res. 1980 Dec;14(12):1339–1342. doi: 10.1203/00006450-198012000-00013. [DOI] [PubMed] [Google Scholar]
  18. Ruzicka F. J., Beinert H. A new iron-sulfur flavoprotein of the respiratory chain. A component of the fatty acid beta oxidation pathway. J Biol Chem. 1977 Dec 10;252(23):8440–8445. [PubMed] [Google Scholar]
  19. Stankovich M. T. An anaerobic spectroelectrochemical cell for studying the spectral and redox properties of flavoproteins. Anal Biochem. 1980 Dec;109(2):295–308. doi: 10.1016/0003-2697(80)90652-1. [DOI] [PubMed] [Google Scholar]
  20. Stankovich M. T., Schopfer L. M., Massey V. Determination of glucose oxidase oxidation-reduction potentials and the oxygen reactivity of fully reduced and semiquinoid forms. J Biol Chem. 1978 Jul 25;253(14):4971–4979. [PubMed] [Google Scholar]
  21. Stankovich M., Fox B. Redox potentials of the flavoprotein lactate oxidase. Biochemistry. 1983 Sep 13;22(19):4466–4472. doi: 10.1021/bi00288a018. [DOI] [PubMed] [Google Scholar]
  22. Steenkamp D. J., Husain M. The effect of tetrahydrofolate on the reduction of electron transfer flavoprotein by sarcosine and dimethylglycine dehydrogenases. Biochem J. 1982 Jun 1;203(3):707–715. doi: 10.1042/bj2030707. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Van Lin B., Bothe H. Flavodoxin from Azotobacter vinelandii. Arch Mikrobiol. 1972;82(2):155–172. doi: 10.1007/BF01890407. [DOI] [PubMed] [Google Scholar]
  24. Vetter H., Jr, Knappe J. Flavodoxin and ferredoxin of Escherichia coli. Hoppe Seylers Z Physiol Chem. 1971 Mar;352(3):433–446. doi: 10.1515/bchm2.1971.352.1.433. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES