Protein carbonylation and metal-catalyzed protein oxidation in a cellular perspective

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperReviewResearchpeer-review

  • Ian Max Møller
  • Adelina Rogowska-Wrzesinska, Department of Biochemistry and Molecular Biology, University of Southern Danmark
  • ,
  • R S P Rao, India
Proteins can become oxidatively modified in many different ways, either by direct oxidation of amino acid side chains and protein backbone or indirectly by conjugation with oxidation products of polyunsaturated fatty acids and carbohydrates. While reversible oxidative modifications are thought to be relevant in physiological processes, irreversible oxidative modifications are known to contribute to cellular damage and disease. The most well-studied irreversible protein oxidation is carbonylation. In this work we first examine how protein carbonylation occurs via metal-catalyzed oxidation (MCO) in vivo and in vitro with an emphasis on cellular metal ion homeostasis and metal binding. We then review proteomic methods currently used for identifying carbonylated proteins and their sites of modification. Finally, we discuss the identified carbonylated proteins and the pattern of carbonylation sites in relation to cellular metabolism using the mitochondrion as a case story.

Original languageEnglish
JournalJournal of Proteomics
Pages (from-to)2228-2242
Number of pages15
Publication statusPublished - 19 Oct 2011

    Research areas

  • Carbonylation, Frataxin, Metal binding, Metal-catalyzed oxidation, Mitochondria, Reactive oxygen species

See relations at Aarhus University Citationformats

ID: 40596960