Fenton Chemistry Revisited: Amino Acid Oxidation

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


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.


Glutamine Synthetase Carbonyl Compound Ternary Complex Isovaleric Acid Fenton Reagent 
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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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