Advanced search
Publication Cover
Free Radical Research Communications Volume 8, 1990 - Issue 4-6
Journal homepage
39
Views
30
CrossRef citations to date
0
Altmetric
Original Article

On The Mechanism Of One-Electron Reduction Of Quinones By Microsomal Flavin Enzymes: The Kinetic Analysis Between Cytochrome B5 And Menadione

Takashi Iyanagi Institute of Basic Medical Sciences, The University of Tsukuba, Ibaraki, 305, Japan
Pages 259-268 | Received 24 Jul 1989, Accepted 25 Aug 1989, Published online: 07 Jul 2009

References

  • Iyanagi T., Yamazaki I. one-electron transfer reactions in biochemical systems III. One-electron reduction of quinones by microsomal flavin enzymes. Biochim. Biophys. Acta 1969; 172: 370–381
  • Iyanagi T., Yamazaki I. One-electron transfer reactions in biochemical system V. Difference in the mechanism of quinone reduction by the NADH-dehydrogenase and the NAD(P)H-dehyd-rogenase (DT-diaphorase). Biochim. Biophys. Acta 1970; 216: 282–294
  • Nishibayashi-Yamashita H., Sato R. Vitamin K3-dependent NADPH Oxidase of liver micro-somes. J. Biochem (Tokyo) 1970; 67: 199–210
  • Bachur N. R., Gordon S. L., Gee M. V., Kon H. NADPH-cytochrome P-450 reductase activation of quinone anticancer agents to free radicals. Proc. Natl. Acad. Sci. USA 1979; 76: 954–957
  • Powis G., Appel P. L. Relationship of the single-electron reduction potential of quinones to their reduction by flavoproteins. Biochem. Pharmacol. 1980; 29: 2567–2572
  • Lind C., Hochstein P., Ernster L. DT-diaphorase as a quinone reductase: A cellular control device against semiquinone and superoxide radical formation. Arch. Biochem. Biophys. 1982; 216: 178–185
  • Svigen B. A., Powis G. Pulse radiolysis studies of antitumor quinones: Radical lifetimes, reactivity with oxygen, and one-electron reduction potential. Arch. Biochem. Biophys. 1981; 209: 119–126
  • Yamazaki I., Ohnishi T. One-electron transfer reactions in biochemical systems I. Kinetic analysis of the oxidation-reduction equilibrium between quinol-quinone and ferro-ferricytochrome c. Biochim. Biophys. Acta 1966; 112: 469–481
  • Sawada Y., Lyanagi T., Yamazaki I. Relation between redox potentials and rate constants in reactions coupled with the system oxygen-superoxide. Biochemistry 1975; 14: 3761–3746
  • Iyanagi T., Mason H. S. Some properties of hepatic reduced nicotinamide adenine dinucleotide phosphate-cytochrome c reductase. Biochemistry 1973; 12: 2297–2308
  • Iyanagi T., Makino R., Anan F. K. Studies on the microsomal mixed-function oxidase system: Mechanism of action of hepatic NADPH-cytochrome P-450 reductase. Biochemistry 1981; 20: 1722–1730
  • Lyanagi T. Redox properties of microsomal reduced nicotinamide adenine dinucleotide-cytochrome b5 reductase and cytochrome b5. Biochemistry 1977; 16: 2725–2730
  • Iyanagi T., Watanabe S., Anan K. F. One-electron oxidation-reduction properties of hepatic NADH-cytochrome b, reductase. Biochemistry 1984; 23: 1418–1425
  • Sawada Y., Ohyama T, Yamazaki I. Preparation and physicochemical properties of green pea superoxide dismutase. Biochim. Biophys. Acta 1972; 268: 305–312
  • Nakamura S., Yamazaki I. One-electron transfer reactions in biochemical systems VII. Two types of electron outlet in milk xanthine oxidase. Biochim. Biophys. Acta 1973; 327: 247–256
  • Makino R., Tanaka T., Iizuka T., Ishimura Y., Kanegasaki S. Stoichiometric Conversion of Oxygen to Superoxide Anion during the Respiratory Burst in Neutrophils: Direct evidence by a new method for measurement of superoxide anion with diacetyldeuteroheme-substituted horseradish peroxidase. J. Biol. Chem. 1986; 261: 11444–11447
  • Ohnishi T., Yamazaki H., Lyanagi T., Nakamura T., Yamazaki I. One-electron transfer reactions in biochemical systems II. The reaction of free radicals formed in the enzymic oxidation. Biochim. Biophys. Acta 1969; 172: 357–369
  • Bielski B. H.J., Arudi R. L. Preparation and stabilization of aqueous/ethanolic superoxide solution. Anal. Biocem. 1983; 133: 170–178
  • Ilan Y. A., Czapski G., Meisel D. The one-electron transfer redox potential of free radicals I. The oxygen/superoxide system. Biochim. Biophys. Acta 1976; 430: 209–224
  • Wood P. W. The potential diagram for oxygen at pH 7. Biochem. J. 1988; 253: 287–289
  • Lyanagi T., Makino N., Mason H. S. Redox properties of the NADPH-cytochrorne P-450 and NADH-cytochrome b, reductases. Biochemistry 1974; 13: 1701–1710
  • Iyanagi T. On the mechanisms of one- and two-electron transfer by flavin enzymes. Chemica Scripta 1987; 27A: 31–36
  • Lübbers D. W., Kessler M., Sholz R., Bücher M. Cytochrome reflection spectra and fluorescence of the isolated. perfused, hemoglobin-free rat liver during a cycle of anoxia. Biochem. Zeitschrift 1965; 341: 346–350
  • Jones D. P., Orrenius S., Mason H. S. Hemoprotein quantitation in isolated hepatocytes. Biochim. Biophys. Acta 1979; 576: 17–29
  • Oshino N. Cytochrome b, and its physiological significance. Pharmacol. Ther. 1978; 2: 477–515
  • Mukeherjee T., Land E. J., Swallow A. J., Bruce J. M. One-electron reduction of Adriamycine and daunomycin: short-term stability of the semiquinones. Arch. Biochem. Biophys. 1989; 225: 116–121

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Order Reprints Request Corporate Permissions

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

Request Academic Permissions

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.

Related research

People also read lists articles that other readers of this article have read.

Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.

Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.