Iron (III) reduction: A novel activity of the human NAD(P)H:oxidoreductase

Biochemical and Biophysical Research Communications

Volumn 353, Issue 2, 2007, Pages 389-393

  Onyenwoke, Rob U ^a   Wiegel, Juergen ^a  

^a UNIVERSITY OF GEORGIA   (United States)

Author keywords

Anaerobic assay; DT diaphorase; Fe(III) reduction; Oxidative stress; Quinone oxidoreductase

Indexed keywords

FERRIC ION; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) DEHYDROGENASE (QUINONE);

ARTICLE; CATALYSIS; ELECTRON TRANSPORT; ENZYME ACTIVITY; ENZYME SUBSTRATE; ISOENZYME ANALYSIS; MICHAELIS CONSTANT; OXIDATION KINETICS; OXIDATIVE STRESS; PRIORITY JOURNAL; STEADY STATE;

CATALYSIS; ENZYME ACTIVATION; HUMANS; IRON; NAD(P)H DEHYDROGENASE (QUINONE); OXIDATION-REDUCTION; SUBSTRATE SPECIFICITY;

EID: 33845779052     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.12.022     Document Type: Article

References (40)

1. Martius C., and Nitz-Litzow D. Demonstration of an in vitro effect of vitamin K1 on oxidative phosphorylation. Biochim. Biophys. Acta 13 (1954) 289-290
2. Maerkif F., and Martius C. Vitamin K reductase from cattle and rat liver. Biochem. Z. 334 (1961) 293-303
3. Ernster L., and Navazio F. Soluble diaphorase in animal tissues. Acta Chem. Scand. 12 (1958) 595-602
4. Hosoda S., Nakamura W., and Hayashi K. Properties and reaction mechanism of DT diaphorase from rat liver. J. Biol. Chem. 249 (1974) 6416-6423
5. Ross D. Quinone reductases: multitasking in the metabolic world. Drug Metabol. Rev. 36 (2004) 639-654
6. Ernster L. DT-diaphorase: a historical review. Chem. Scr. 27A (1987) 1-13
7. Faig M., Bianchet M.A., Talalay P., Chen S., Winski S., Ross D., and Amzel L.M. Structures of recombinant human and mouse NAD(P)H:quinone oxidoreductases: species comparison and structural changes with substrate binding and release. Proc. Natl. Acad. Sci. USA 97 (2000) 3177-3182
8. Smith D., Martin L.F., and Wallin R. Human DT-diaphorase, a potential cancer protecting enzyme. Its purification from abdominal adipose tissue. Cancer Lett. 42 (1988) 103-112
9. Cavelier G., and Amzel L.M. Mechanism of NAD(P)H:quinone reductase: Ab initio studies of reduced flavin. Proteins 43 (2001) 420-432
10. Prochaska H.J. Purification and crystallization of rat liver NAD(P)H:(quinone-acceptor) oxidoreductase by cibacron blue affinity chromatography: identification of a new and potent inhibitor. Arch. Biochem. Biophys. 267 (1988) 529-538
11. Iyanagi T., and Yamazaki I. One-electron-transfer reactions in biochemical systems. V. Difference in the mechanism of quinone reduction by the NADH dehydrogenase and the NAD(P)H dehydrogenase (DT-diaphorase). Biochim. Biophys. Acta 216 (1970) 282-294
12. Powis G., and Appel P.L. Relationship of the single-electron reduction potential of quinones to their reduction by flavoproteins. Biochem. Pharmacol. 29 (1980) 2567-2572
13. Cui K., Lu A.Y., and Yang C.S. Subunit functional studies of NAD(P)H:quinone oxidoreductase with a heterodimer approach. Proc. Natl. Acad. Sci. USA 92 (1995) 1043-1047
14. Siegel D., Gustafson D.L., Dehn D.L., Han J.Y., Boonchoong P., Berliner L.J., and Ross D. NAD(P)H:quinone oxidoreductase 1: role as a superoxide scavenger. Mol. Pharmacol. 65 (2004) 1238-1247
15. Petrilli F.L., and de Flora S. Metabolic reduction of chromium as a threshold mechanism limiting its in vivo activity. Sci. Total Environ. 71 (1988) 357-364
16. Aiyar J., de Flora S., and Wetterhahn K.E. Reduction of chromium(VI) to chromium(V) by rat liver cytosolic and microsomal fractions: is DT-diaphorase involved?. Carcinogenesis 13 (1992) 1159-1166
17. Levis A.G., and Bianchi V. Mutagenic and cytogenetic effects of chromium compounds. In: Langard S. (Ed). Biological and Environmental Effects of Chromium (1982), Elsevier Biomedical Press, New York, NY 171-208
18. Viamajala S., Peyton B.M., Sani R.K., Apel W.A., and Petersen J.N. Toxic effects of chromium(VI) on anaerobic and aerobic growth of Shewanella oneidensis MR-1. Biotechnol. Prog. 20 (2004) 87-95
19. Yassi A., and Nieboer E. Carcinogenicity of chromium compounds. In: Nriagu J.O., and Nieboer E. (Eds). Chromium in the Natural and Human Environments (1988), John Wiley and Sons, New York, NY 443-496
20. Hayes R.B. The carcinogenicity of metals in humans. Cancer Causes Control 8 (1997) 371-385
21. Stearns D.M., Belbruno J.J., and Wetterhahn K.E. A prediction of chromium (III) accumulation in humans from chromium dietary supplements. FASEB J. 9 (1995) 1650-1657
22. Andrews N.C., Fleming M.D., and Gunshin H. Iron transport across biological membranes. Nutr. Rev. 57 (1999) 114-123
23. Zigler J.S., Jernigan H.M., Garland D., and Reddy V.N. The effects of "oxygen radicals" generated in the medium on lenses in organ culture: inhibition of damage by chelated iron. Arch. Biochem. Biophys. 241 (1985) 163-172
24. Gutteridge J.M., and Halliwell B. Free radicals and antioxidants in the year 2000. A historical look to the future. Ann. N. Y. Acad. Sci. 899 (2000) 136-147
25. 2 by NAD(P)H-flavin oxidoreductase and 4-hydroxyphenylacetate 3-monooxygenase. Biochemistry 42 (2003) 7509-7517
26. Beall H.D., Mulcahy R.T., Siegel D., Traver R.D., Gibson N.W., and Ross D. Metabolism of bioreductive antitumor compounds by purified rat and human DT-diaphorases. Cancer Res. 54 (1994) 3196-3201
27. Ljungdahl L.G., and Wiegel J. Working with anaerobic bacteria. In: Demain A.L., and Solomon N.A. (Eds). Manual of Industrial Microbiology and Biotechnology (1986), American Society for Microbiology, Washington, DC 84-96
28. Dailey H.A., and Lascelles J. Reduction of iron and synthesis of protoheme by Spirillum itersonii and other organisms. J. Bacteriol. 129 (1977) 815-820
29. Ernster L., Danielson L., and Ljunggren M. DT diaphorase. I. Purification from the soluble fraction of rat-liver cytoplasm, and properties. Biochim. Biophys. Acta 58 (1962) 171-188
30. Cleland W.W. Determining the chemical mechanisms of enzyme-catalyzed reactions by kinetic studies. Adv. Enzymol. Relat. Areas Mol. Biol. 45 (1977) 273-387
31. Segel I.H. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady State Enzyme Systems (1975), John Wiley & Sons, Inc., Toronto, Canada
32. Mazoch J., Tesarik R., Sedlacek V., Kucera I., and Turanek J. Isolation and biochemical characterization of two soluble iron (III) reductases from Paracoccus denitrificans. Eur. J. Biochem. 271 (2004) 553-562
33. Kaufmann F., and Lovley D.R. Isolation and characterization of a soluble NADPH-dependent Fe(III) reductase from Geobacter sulfurreducens. J. Bacteriol. 183 (2001) 4468-4476
34. Bae W.C., Lee H.K., Choe Y.C., Jahng D.J., Lee S.H., Kim S.J., Lee J.H., and Jeong B.C. Purification and characterization of NADPH-dependent Cr(VI) reductase from Escherichia coli ATCC 33456. J. Microbiol. 43 (2005) 21-27
35. Li R., Bianchet M.A., Talalay P., and Amzel L.M. The three-dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: mechanism of the two-electron reduction. Proc. Natl. Acad. Sci. USA 92 (1995) 8846-8850
36. Sparla F., Preger V., Pupillo P., and Trost P. Characterization of a novel NADH-specific, FAD-containing, soluble reductase with ferric citrate reductase activity from maize seedlings. Arch. Biochem. Biophys. 363 (1999) 301-308
37. Fontecave M., Coves J., and Pierre J.L. Ferric reductases or flavin reductases?. Biometals 7 (1994) 3-8
38. 2 status during the third trimester of pregnancy. J. Am. Coll. Nutr. 18 (1999) 324-329
39. Dale S.E., Doherty-Kirby A., Lajoie G., and Heinrichs D.E. Role of siderophore biosynthesis in virulence of Staphylococcus aureus: identification and characterization of genes involved in production of a siderophore. Infect. Immun. 72 (2004) 29-37
40. Dicker E., and Cederbaum A.I. Requirement for iron for the production of hydroxyl radicals by rat liver quinone reductase. J. Pharmacol. Exp. Ther. 266 (1993) 1282-1290