Advertisement
Journal of Biological Chemistry
Open access logo
Advanced searchSave search
OXIDATION-REDUCTION AND BIOENERGETICS| Volume 246, ISSUE 22, P6886-6890, November 25, 1971

Download started.

Ok

The Generation of Superoxide Radical during the Autoxidation of Ferredoxins

Open AccessPublished:November 25, 1971DOI:https://doi.org/10.1016/S0021-9258(19)45929-2
The Generation of Superoxide Radical during the Autoxidation of Ferredoxins
Previous ArticleEffect of Silicotungstate on Reduced Diphosphopyridine Nucleotide Oxidation in Submitochondrial Particles
Next ArticleEnzymes That Hydrolyze Fungal Cell Wall Polysaccharides
      This paper is only available as a PDF. To read, Please Download here.
      Clostridial and spinach ferredoxins, reduced enzymatically by the action of ferredoxin-TPN+ oxidoreductase, have been shown to carry out the univalent reduction of oxygen. The superoxide radicals, so generated, were detected by their ability to cause the oxidation of epinephrine to adrenochrome. Superoxide dismutase prevented the production of adrenochrome in these reaction mixtures, while having no effect on the rate of oxidation of TPNH. The ratio of the univalent reduction of oxygen to the sum of the univalent plus divalent reductions of oxygen was computed as a function of pH and of the concentrations of oxygen. This percentage of univalent flux increased with rising pH and with increasing concentrations of oxygen as has previously been observed in the case of milk xanthine oxidase. Under comparable conditions of pH and of oxygen concentration, milk xanthine oxidase generated O2- four times more rapidly than did clostridial ferredoxin.

      REFERENCES

        • McCord J.M.
        • Fridovich I.
        J. Biol. Chem. 1968; 243: 5753
        • McCord J.M.
        • Fridovich I.
        Fed. Proc. 1969; 28: 346
        • McCord J.M.
        • Fridovich I.
        J. Biol. Chem. 1969; 244: 6049
        • Knowles P.F.
        • Gibson J.F.
        • Pick F.M.
        • Bray II., C.
        Biochem. J. 1969; III: 53
        • Massey V.
        • Strickland S.
        • Mayhew S.G.
        • Howell L.G.
        • Engel P.C.
        • Matthews R.G.
        • Schuman M.
        • Süllivan P.A.
        Biochem. Biophys. Res. Commun. 1969; 36: 891
        • Rajagopalan K.V.
        • Handler P.
        Singer T.P. Biological oxidations. Interscierice Publishers, Inc., New York1968: 301
        • McCord J.M.
        • Fridovich I.
        J. Biol. Chem. 1969; 244: 6056
        • Fridovich I.
        J. Biol. Chem. 1970; 245: 4053
        • Petering D.H.
        • Palmer G.
        Arch. Biochem. Biophys. 1970; 141: 456
        • Davis B.J.
        Ann. N. Y. Acad. Sci. 1964; 121: 404
        • Petering D.
        • Fee J.A.
        • Palmee G.
        J. Biol. Chem. 1971; 246: 643
        • San Pietro A.
        Colowicic S.P. Kaplan N.O. Methods in enzumoloqy. 6. Academic Press, New York1963: 439
        • Moss T.H.
        • Petering D.
        • Palmer G.
        J. Biol. Chem. 1969; 244: 2275
        • Tagawa K.
        • Arnon D.I.
        Biochim. Biophys. Acta. 1968; 153: 602
        • Shin M.
        • Tagawa K.
        • Arnon D.I.
        Biochem. Z. 1963; 338: 84
        • Brady F.O.
        Ph. D. Thesis. Duke University, 1969
        • Lazarow A.
        • Cooperstein S.J.
        Science. 1954; 120: 674
        • Green S.
        • Mazur A.
        • Shorr E.
        J. Biol. Chem. 1956; 220: 237
        • Foust G.P.
        • Mayhew S.G.
        • Massey V.
        J. Biol. Chem. 1969; 244: 964
        • Beinert H.
        San Pietro A. Nonheme iron proteins: role in energy conversion. The Antioch Press, Yellow Springs, Ohio1965: 23
        • Britzinger H.
        • Palmer G.
        • Sands R.H.
        Biochemistry. 1966; 55: 397
        • Tsibris J.C.M.
        • Tsai R.L.
        • Gunsalus I.C.
        • Orme-John-son W.H.
        • Hansen R.E.
        • Beinert H.
        Proc. Nat. Acad. Sci. U. S. A. 1968; 59: 5959
        • Orme-Johnson W.H.
        • Hansen R.E.
        • Beinert H.
        • Tsibris J.C.M.
        • Bartholomaus R.C.
        • Gunsalus I.C.
        Proc. Nat. Acad. Sci. U. S. A. 1968; 60: 368
        • Johnson C.E.
        • Commack R.
        • Rao K.K.
        • Hall D.O.
        Biochem. Biophys. Res. Commun. 1971; 43: 564
        • Orme-Johnson W.H.
        • Beinert H.
        Biochem. Biophys. Res. Commun. 1969; 36: 905
        • Nilsson R.
        • Pick F.M.
        • Bray R.C.
        Biochim. Biophys. Acta. 1969; 192: 145
        • Mayhew S.G.
        • Petering D.
        • Palmer G.
        • Foust G.P.
        J. Biol. Chem. 1969; 244: 2830
        • Evans M.C.W.
        • Hall D.O.
        • Bothe H.
        • Whatley F.R.
        Biochem. J. 1968; 110: 485
        • Nelson N.
        • Neumann J.
        Biochem. Biophys. Res. Commun. 1968; 30: 142
      30. J. Biol. Chem. 1969; 244 (1932): 1926

      Article info

      Publication history

      Published online: November 25, 1971
      Received: July 12, 1971

      Identification

      DOI: https://doi.org/10.1016/S0021-9258(19)45929-2

      Copyright

      © 1971 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.

      User license

      Creative Commons Attribution (CC BY 4.0) |
      How you can reuse Information Icon
      Creative Commons Attribution (CC BY 4.0)

      Permitted

      • Read, print & download
      • Redistribute or republish the final article
      • Text & data mine
      • Translate the article
      • Reuse portions or extracts from the article in other works
      • Sell or re-use for commercial purposes

      Elsevier's open access license policy

      ScienceDirect

      Access this article on ScienceDirect

      ASBMB  ASBMB  ASBMB  ASBMB

      ISSN 0021-9258
      We use cookies to help provide and enhance our service and tailor content. To update your cookie settings, please visit the for this site.
      Copyright © 2022 Elsevier Inc. except certain content provided by third parties. The content on this site is intended for healthcare professionals.


      RELX