title: Implication of protein oxidation in protein turnover, aging, and oxygen toxicity.
abstract: It is evident from the results summarized here that a variety of MFO systems catalyze the oxidation inactivation of enzymes. This likely involves site-directed Fenton-chemistry in which Fe(II) bound to metal binding sites on the protein undergoes peroxidation to form active oxygen species that convert proximal amino acid residues to carbonyl derivatives. Such oxidation is likely involved in the accumulation of altered enzymes during aging, in premature aging diseases, in the killing of bacteria by neutrophils and in protein turnover. In view of these results, the possibility that protein oxidation is implicated in various diseases, viz, arthritis, pulmonary dysfunction, and carcinogenesis deserves consideration.
authors.affiliation: Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, Bethesda, Maryland 20892.
authors.forename: E R
authors.initials: ER
authors.lastname: Stadtman
authors.forename: C N
authors.initials: CN
authors.lastname: Oliver
authors.forename: R L
authors.initials: RL
authors.lastname: Levine
authors.forename: L
authors.initials: L
authors.lastname: Fucci
authors.forename: A J
authors.initials: AJ
authors.lastname: Rivett
mesh_terms: D000375:Aging; D000818:Animals; D004492:Edetic Acid / Q000494:pharmacology; D004795:Enzyme Stability; D004798:Enzymes / Q000378:metabolism*; D010100:Oxygen / Q000494:pharmacology / Q000633:toxicity*; D010455:Peptides
chemical_list: D004798:Enzymes; D010455:Peptides; D004492:Edetic Acid; D010100:Oxygen