Title : Characterization of adducts of ethanol metabolites with cytochrome c.

Pub. Date : 1999 Jan

PMID : 10029200






3 Functional Relationships(s)
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1 We report that addition of ethanol to this system of cyt c plus peroxide results in replacement of the Tyr/Trp radicals by 1-hydroxyethyl radicals (HER), and covalent binding of up to 10 mol of ethanol per mol of cyt c. Tryptophan cytochrome c, somatic Homo sapiens
2 Structural analysis by mass spectrometry of the tryptic digestion fractions of adducted cyt c is consistent with several peptides bearing one-to-three acetaldehyde moieties on Lys residues, and three distinct Tyr/Trp-containing peptides: P[28-53], P[56-73], P[73-91] carrying one-to-two HER. Tryptophan cytochrome c, somatic Homo sapiens
3 The x-ray crystallographic structure of cyt c shows that the Tyr/Trp residues in the adducted peptides are in close proximity to the heme. Tryptophan cytochrome c, somatic Homo sapiens