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Protein self-modification by heme-generated reactive species.
- Source :
-
IUBMB life [IUBMB Life] 2008 Jan; Vol. 60 (1), pp. 41-56. - Publication Year :
- 2008
-
Abstract
- In the presence of H(2)O(2), heme proteins form active intermediates, which are able to oxidize exogenous molecules. Often these products are not stable compounds but reactive species on their own, such as organic radicals. They can both diffuse to the bulk of the solution or react with the protein that generated them. Here, we describe the self-modification underwent by heme proteins with globin-type fold, that is, myoglobin, hemoglobin, and neuroglobin when treated with NO(2) (-) or catechols in the presence of H(2)O(2). The reactive nitrogen species generated by NO(2) (-) give rise to nitration, oxidation, and/or crosslinking reactions between the proteins or their subunits. The quinones formed upon reaction with catechols easily modify Cys and His residues and eventually cause protein aggregation, which induces precipitation. The pattern of modifications undergone by the protein strongly depends on the nature of the protein and the reaction conditions.
- Subjects :
- Amino Acid Sequence
Catechols chemistry
Catechols metabolism
Dopamine metabolism
Globins physiology
Hemeproteins chemistry
Humans
Models, Molecular
Myoglobin metabolism
Nerve Tissue Proteins physiology
Neuroglobin
Nitrites metabolism
Nitrogen Dioxide metabolism
Quinones metabolism
Hemeproteins physiology
Reactive Nitrogen Species metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1521-6543
- Volume :
- 60
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- IUBMB life
- Publication Type :
- Academic Journal
- Accession number :
- 18379991
- Full Text :
- https://doi.org/10.1002/iub.10