Measurement of the Oxidation-reduction Potentials for One-electron and Two-electron Reduction of Electron-transfer Flavoprotein from Pig Liver

Overview

Journal Biochem J

Specialty Biochemistry

Date 1984 May 1

PMID 6743239

Citations 12

Authors

M Husain

M T Stankovich

B G Fox

Affiliations

Soon will be listed here.

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.

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References

Mayhew S, MASSEY V . Purification and characterization of flavodoxin from Peptostreptococcus elsdenii. J Biol Chem. 1969; 244(3):794-802. View

Vetter Jr H, Knappe J . Flavodoxin and ferredoxin of Escherichia coli. Hoppe Seylers Z Physiol Chem. 1971; 352(3):433-46. DOI: 10.1515/bchm2.1971.352.1.433. View

Van Lin B, Bothe H . Flavodoxin from Azotobacter vinelandii. Arch Mikrobiol. 1972; 82(2):155-72. DOI: 10.1007/BF01890407. View

OReilly J . Oxidation-reduction potential of the ferro-ferricyanide system in buffer solutions. Biochim Biophys Acta. 1973; 292(3):509-15. DOI: 10.1016/0005-2728(73)90001-7. View

Hall C, 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; 250(9):3476-86. View

Ruzicka F, BEINERT H . A new iron-sulfur flavoprotein of the respiratory chain. A component of the fatty acid beta oxidation pathway. J Biol Chem. 1977; 252(23):8440-5. View

Stankovich M, Schopfer L, MASSEY V . Determination of glucose oxidase oxidation-reduction potentials and the oxygen reactivity of fully reduced and semiquinoid forms. J Biol Chem. 1978; 253(14):4971-9. View

McKean M, Frerman F, Mielke D . General acyl-CoA dehydrogenase from pig liver. Kinetic and binding studies. J Biol Chem. 1979; 254(8):2730-5. View

Hall C, Lambeth J . Studies on electron transfer from general acyl-CoA dehydrogenase to electron transfer flavoprotein. J Biol Chem. 1980; 255(8):3591-5. View

10.

Noda C, Rhead W, 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; 77(5):2646-50. PMC: 349459. DOI: 10.1073/pnas.77.5.2646. View

11.

Reinsch J, Feinberg B, McFarland J . Intermediates during the fatty acyl CoA dehydrogenase catalyzed reduction of electron transfer flavoprotein (ETF) by fatty acyl CoA esters. Biochem Biophys Res Commun. 1980; 94(4):1409-16. DOI: 10.1016/0006-291x(80)90576-8. View

12.

Choong Y, MASSEY V . Stabilization of lactate oxidase flavin anion radical by complex formation. J Biol Chem. 1980; 255(18):8672-7. View

13.

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; 14(12):1339-42. DOI: 10.1203/00006450-198012000-00013. View

14.

Stankovich M . An anaerobic spectroelectrochemical cell for studying the spectral and redox properties of flavoproteins. Anal Biochem. 1980; 109(2):295-308. DOI: 10.1016/0003-2697(80)90652-1. View

15.

Beckmann J, Frerman F, McKean M . Inhibition of general acyl CoA dehydrogenase by electron transfer flavoprotein semiquinone. Biochem Biophys Res Commun. 1981; 102(4):1290-4. DOI: 10.1016/s0006-291x(81)80151-9. View

16.

Steenkamp D, Husain M . The effect of tetrahydrofolate on the reduction of electron transfer flavoprotein by sarcosine and dimethylglycine dehydrogenases. Biochem J. 1982; 203(3):707-15. PMC: 1158287. DOI: 10.1042/bj2030707. View

17.

McKean M, Beckmann J, Frerman F . Subunit structure of electron transfer flavoprotein. J Biol Chem. 1983; 258(3):1866-70. View

18.

Gorelick R, Mizzer J, Thorpe C . Purification and properties of electron-transferring flavoprotein from pig kidney. Biochemistry. 1982; 21(26):6936-42. DOI: 10.1021/bi00269a049. View

19.

Husain M, Steenkamp D . Electron transfer flavoprotein from pig liver mitochondria. A simple purification and re-evaluation of some of the molecular properties. Biochem J. 1983; 209(2):541-5. PMC: 1154123. DOI: 10.1042/bj2090541. View

20.

Stankovich M, Fox B . Redox potentials of the flavoprotein lactate oxidase. Biochemistry. 1983; 22(19):4466-72. DOI: 10.1021/bi00288a018. View