Electrochemical behaviour of human adrenodoxin on a pyrolytic graphite electrode

Bioelectrochemistry

Volumn 59, Issue 1-2, 2003, Pages 41-47

  Johnson, Daniel ^a   Norman, Shona ^a   Tuckey, Robert C ^b   Martin, Lisandra L ^a  

^a FLINDERS UNIVERSITY   (Australia)

^b UNIVERSITY OF WESTERN AUSTRALIA   (Australia)

Author keywords

Adrenodoxin; Cyclic voltammetry; Human; Metalloprotein; Pyrolytic graphite; 2Fe2S centres

Indexed keywords

ELECTROCHEMISTRY; ENZYME IMMOBILIZATION; GRAPHITE ELECTRODES; PROTEINS; REDOX REACTIONS;

ELECTRON TRANSFER;

BIOCHEMISTRY;

ADRENODOXIN; CYTOCHROME P450; GRAPHITE; POLYLYSINE;

ANALYTIC METHOD; ARTICLE; CORRELATION ANALYSIS; ELECTRICITY; ELECTROCHEMICAL ANALYSIS; ELECTRON; ELECTRON TRANSPORT; OXIDATION REDUCTION REACTION; PH;

EID: 0037389622     PISSN: 15675394     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1567-5394(02)00188-3     Document Type: Article

References (30)

1. Lambeth J.D., Seybert D.W., Lancaster J.R., Salerno J.C., Kamin H. Steroidogenic electron transport in adrenal cortex mitochondria. Mol. Cell. Biochem. 45:1982;13-31.
2. Vickery L.E. Molecular recognition and electron transfer in mitochondrial steroid hydroxylase systems. Steroids. 62:1997;124-127.
3. Bernhardt R. Cytochrome P450: structure, function, and generation of reactive oxygen species. Rev. Physiol., Biochem. Pharmacol. 127:1996;137-221.
4. Schwarz D., Chernogolov A., Kisselev P. Complex formation in vesicle-reconstituted mitochondrial cytochrome P450 systems (CYP11A1 and CYP11B1) as evidenced by rotational diffusion experiments using EPR and ST-EPR. Biochemistry. 38:1999;9456-9464.
5. Bernhardt R. Cytochrome P450: structure, function, and generation of reactive oxygen species. Rev. Physiol., Biochem. Pharmacol. 127:1996;137-221.
6. Pascoe L., Curnow K.M., Slutsker L., Rosler A., White P.C. Mutations in the human CYP11B2 (aldosterone synthase) causing corticosterone methyloxidase II deficiency. Proc. Natl. Acad. Sci. U. S. A. 89:1992;4996-5000.
7. Lill R., Kispal G. Maturation of cellular Fe-S proteins: an essential function of mitochondria. Trends Biochem. Sci. 25:2000;352-356.
8. Tuckey R.C., Kaimin H. The oxyferro complex of adrenal cytochrome P-450scc. Effect of cholesterol and intermediates on its stability and optical characteristics. J. Biol. Chem. 257:1982;9309-9314.
9. Tuckey R.C., Kaimin H. Kinetics of incorporation of adrenal cytochrome P-450scc into phosphatidylcholine vesicles. J. Biol. Chem. 257:1982;2887-2893.
10. Hume R., Kelly R.W., Taylor P.L., Boyd G.S. The catalytic cycle of cytochrome P-450scc and intermediates in the conversion of cholesterol to pregnenolone. Eur. J. Biochem. 140:1984;583-591.
11. Tuckey R.C., Sadleir J. The concentration of adrenodoxin reductase limits cytochrome P450scc activity in the human placenta. Eur. J. Biochem. 263:1999;319-325.
12. Tuckey R.C., McKinley A.J., Headlam M.J. Oxidized adrenodoxin acts as a competitive inhibitor of cytochrome P450scc in mitochondria from the human placenta. Eur. J. Biochem. 268:2001;2338-2343.
13. Liscomb J.D., Sligar S.G., Namtvedt M.J., Gunsalus I.C. Autooxidation and hydroxylation reactions of oxygenated cytochrome P-450cam. J. Biol. Chem. 251:1976;1116-1124.
14. Armstrong F.A. Probing metalloproteins by voltammetry. Struct. Bond. 72:1990;137-221.
15. Armstrong F.A., Wilson G.S. Recent developments in faradic bioelectrochemistry. Electrochim. Acta. 45:2000;2623-2645.
16. 4S] cluster. J. Biol. Chem. 268:1993;25928-25939.
17. 4S] cluster of Azotobacter vinelandii ferredoxin: I. J. Am. Chem. Soc. 115:1993;12587-12588.
18. Jin W., Wollenberger U., Bernhardt R., Stocklein W.F.M., Scheller F.W. Direct electron transfer of adrenodoxin - a [2Fe-2S] protein - and its mutants at modified gold electrode. Bioelectrochem. Bioenerg. 47:1998;75-79.
19. Wong L.S., Vilker V.L. Direct electrochemistry of putidaredoxin at a modified gold electrode. J. Electroanal. Chem. 389:1995;201-203.
20. Johnson D.L., Maxwell C.J., Losic D., Shapter J.G., Martin L.L. The influence of promotor and of electrode material on the cyclic voltammetry of Pisum sativum plastocyanin. Bioelectrochemistry. 58/2:2002;137-147.
21. Woods S.T., Sadleir J., Downs T., Triantopoulos T., Headlam M.J., Tuckey R.C. Expression of catalytically active human cytochrome P450scc in Escherichia coli and mutagenesis of isoleucine-462. Arch. Biochem. Biophys. 353:1998;109-115.
22. Huang J.J., Kimura T. Studies on adrenal steroid hydroxylases. Oxidation reduction properties of adrenal iron-sulfur protein (adrenodoxin). Biochemistry. 12:1973;406-409.
23. Mittal S., Zhu Y.-Z., Vickery L.E. Molecular cloning and sequence analysis of human placental ferredoxin. Arch. Biochem. Biophys. 264:1988;383-391.
24. Laviron E. General expression of the linear potential sweep voltammogram in the case of diffusionless electrochemical system. J. Electroanal. Chem. 101:1979;19-28.
25. Armstrong F.A., Heering H.A., Hirst J. Reactions of complex metalloproteins studied by protein-film voltammetry. Chem. Soc. Rev. 26:1997;169-179.
26. Green L.M., O'Brien P., Stonehurerner J., Millett F. Identification of specific carboxylate groups on adrenodoxin that are involved in the interaction with adrenodoxin reductase. J. Biol. Chem. 259:1984;2155-2160.
27. Coghlan V.M., Vickery L.E. Site-specific mutations in human ferredoxin that affect the binding to ferredoxin reductase and cytochrome P450scc. J. Biol. Chem. 266:1991;18606-18612.
28. Lambeth J.D., Kaim H. Adrenodoxin reductase-adrenodoxin complex. Flavin to iron-sulfur electron transfer as the rate-limiting step in the NADPH-cytochrome c reductase reaction. J. Biol. Chem. 254:1979;2766-2774.
29. Beilke D., Weiss R., Lohr F., Pristovsek P., Hannemann F., Bernhardt R., Ruterjans H. A new electron transport mechanism in mitochondrial steroid hydroxylase systems based on structural changes upon the reduction of adrenodoxin. Biochem. 41:2002;7969-7978.
30. Lu Z., Lvov Y., Jansson I., Schenkman J.B., Rusling R.F. Electroactive films of alternate layered polycations and iron-sulfur protein putidaredoxin on gold. J. Colloid Interface Sci. 224:2000;162-168.