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Fenton Chemistry Revisited: Amino Acid Oxidation

  • E. R. Stadtman
  • B. S. Berlett
Part of the Basic Life Sciences book series (BLSC, volume 49)

Abstract

Many mixed-function oxidation (MFO) systems catalyze the O2/Fe(II)-dependent oxidative inactivation of enzymes.1–5 Such oxidation is likely implicated in the regulation of enzyme degradation2,5–7 in the accumulation of altered forms of enzymes during aging8,9 in neutrophil function.10 Results of mechanistic studies indicate that MFO systems generate H2O2 and Fe(II) which interact at metal-binding sites on the protein to generate active oxygen species (•OH, perferryl ion, singlet oxygen); the activated oxygen reacts in situ with the side chains of proximal amino acid residues (especially with histidine, arginine, proline, and lysine residues) and converts them to carbonyl derivatives.1,3,11 Protein oxidation by MFO systems is thus attributable to Fenton chemistry that occurs at Fe(II) binding sites on the protein.

Keywords

Glutamine Synthetase Carbonyl Compound Ternary Complex Isovaleric Acid Fenton Reagent 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. 1.
    L. Fucci, C. N. Oliver, M. J. Coon, and E. R. Stadtman, Inactivation of key metabolic enzymes by mixed-function oxidation reactions: Possible implication in protein turnover and ageing, Proc. Natl. Acad, Sci, U.S.A. 80:1521 (1983).CrossRefGoogle Scholar
  2. 2.
    C. N. Oliver, R. L. Levine, and E. R. Stadtman, Regulation of glutamine synthetase degradation, In: “Experiences in Biochemical Perception,” L. N. Ornston and S. G. Sligar, eds., Academic Press, New York (1982).Google Scholar
  3. 3.
    R. L. Levine, Oxidative modification of glutamine synthetase. II. Characterization of the ascorbate model system, J. Biol. Chem. 258:11828 (1983).PubMedGoogle Scholar
  4. 4.
    K. Kim, S. G. Rhee, and E. R. Stadtman, Nonenzymatic cleavage of proteins by reactive oxygen species generated by dithiothreitol and iron, J. Biol. Chem. 260:15394 (1985).PubMedGoogle Scholar
  5. 5.
    R. L. Levine, C. N. Oliver, R. M. Fulks, and E. R. Stadtman, Turnover of bacterial glutamine synthetase: Oxidative inactivation precedes proteolysis, Proc. Natl. Acad. Sci. U.S.A. 78:2120 (1981).PubMedCrossRefGoogle Scholar
  6. 6.
    A. J. Rivett, Preferential degradation of the oxidatively modified form of glutamine synthetase by intracellular mammalian proteases, J. Biol. Chem. 260:300 (1985).PubMedGoogle Scholar
  7. 7.
    A. J. Rivett, J. E. Roseman, C. N. Oliver, R. L. Levine, and E. R. Stadtman, Covalent modification of proteins by mixed-function oxidation: Recognition by intracellular proteases, in: “Intracellular Protein Catabolism,” E. A. Khairallah, J. S. Bond, and J. W. C. Bird, eds., Alan R. Liss, New York (1985).Google Scholar
  8. 8.
    C. N. Oliver, B. Ahn, M. E. Wittenberger, R. L. Levine, and E. R. Stadtman, Age-related alterations of enzymes may involve mixed-function oxidation reactions, in: “Modification of Proteins during Aging,” R. C. Adelman and E. R. Dekker, eds., Alan R. Liss, New York (1985).Google Scholar
  9. 9.
    C. N. Oliver, B.-W. Ahn, E. J. Moerman, S. Goldstein, and E. R. Stadtman, Age-related changes in oxidized proteins, J. Biol. Chem. 262:5488 (1987).PubMedGoogle Scholar
  10. 10.
    C. N. Oliver, Inactivation of enzymes and oxidative modification of proteins by stimulated neutrophils, Arch. Biochem. Biophys. 253: 62 (1987).PubMedCrossRefGoogle Scholar
  11. 11.
    C. N. Oliver, B. Ahn, M. E. Wittenberger, and E. R. Stadtman, Oxidative inactivation of enzymes: Implication in protein turnover and aging, in: “Cellular Regulation and Malignant Growth,” S. Ebashi, ed., Japan Scientific Societies Press, Tokyo/Springer-Verlag, Berlin (1985).Google Scholar
  12. 12.
    I. Zs-Nagy and R. A. Floyd, Hydroxyl free radical reaction with amino acids and proteins studied by electron spin resonance spectroscopy and spin-trapping, Biochim. Biophys. Acta 790:238 (1984).CrossRefGoogle Scholar
  13. 13.
    J. M. C. Gutteridge, R. Richmond, and B. Halliwell, Inhibition of the iron-catalyzed formation of hydroxyl radicals from superoxide and of lipid peroxidation by desferrioxamine, Biochem. J. 184:469 (1979).PubMedGoogle Scholar

Copyright information

© Plenum Press, New York 1988

Authors and Affiliations

  • E. R. Stadtman
    • 1
  • B. S. Berlett
    • 1
  1. 1.Laboratory of Biochemistry, National Heart, Lung, and Blood InstituteNational Institutes of HealthBethesdaUSA

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