Protein self-modification by heme-generated reactive species.

Protein self-modification by heme-generated reactive species. Research Abstract Details 

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Protein self-modification by heme-generated reactive species. Abstract Text:

Enrico Monzani,Stefania Nicolis,Raffaella Roncone,Marica Barbieri,Alessandro Granata,Luigi Casella,Enrico Monzani,Stefania Nicolis,Raffaella Roncone,Marica Barbieri,Alessandro Granata,Luigi Casella,

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. (c) 2007 IUBMB IUBMB Life, 60(1): 41-56, 2008.

Protein self-modification by heme-generated reactive species. Publishing Authors By Initials

E Monzani,S Nicolis,R Roncone,M Barbieri,A Granata,L Casella,E Monzani,S Nicolis,R Roncone,M Barbieri,A Granata,L Casella,

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Protein self-modification by heme-generated reactive species. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: IUBMB life

VOLUME: 60

Page Numbers: 41-56

Journal Abbreviation: IUBMB Life

ISSN: 1521-6543

DAY: 1

MONTH: Jan

YEAR: 2008

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LANGUAGE: eng

NlmUniqueID: 100888706

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Grant and Affiliation Information for Protein self-modification by heme-generated reactive species.

AFFILIATION: Dipartimento di Chimica Generale, Via Taramelli 12, Pavia, Italy.

Country: England

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MEDLINETA: IUBMB Life

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