Evidence for a slow and oxygen-insensitive intra-molecular long range electron transfer from tyrosine residues to the semi-oxidized tryptophan 214 in human serum albumin: its inhibition by bound copper (II) |
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Authors: | Larry K Patterson Jean-Claude Mazière David M Bartels Gordon L Hug René Santus " target="_blank">Patrice Morlière |
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Institution: | 1.Radiation Laboratory,University of Notre Dame,Notre Dame,USA;2.Laboratoire de Biochimie,CHU Amiens,Amiens,France;3.Faculté de Médecine et de Pharmacie, EA4292,Université de Picardie Jules Verne,Amiens,France;4.INSERM, ERI12,Amiens,France;5.Laboratoire de Biochimie,INSERM ERI 12, CHU Amiens, H?pital Nord,Amiens Cedex 01,France;6.Département RDDM,Muséum National d’Histoire Naturelle,Paris,France |
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Abstract: | A slow, long range electron transfer (SLRET) in human serum albumin (HSA) is observed from an intact tyrosine (Tyr) residue
to the neutral tryptophan (Trp) radical (Trp·) generated in pulse radiolysis. This radical is formed, at neutral pH, through
oxidation with Br2·− radical anions of the single Trp 214 present. The SLRET rate constant of ~0.2 s−1 determined is independent of HSA concentration and radiation dose, consistent with an intra-molecular process. This is the
slowest rate constant so far reported for an intra-molecular LRET. In sharp contrast with the LRET reported for other proteins,
the SLRET observed here is insensitive to oxygen, suggesting that the oxidized Trp is inaccessible to—or do not react with
radiolytically generated O2·−. In N2O-saturated solutions, the SLRET is inhibited by Cu2+ ions bound to the His 3 residue of the N-terminal group of HSA but it is partially restored in O2-saturated solutions. |
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