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Title: CO sub 2 ter dot minus radical induced cleavage of disulfide bonds in proteins. A gamma-ray and pulse radiolysis mechanistic investigation

Journal Article · · Biochemistry; (USA)
DOI:https://doi.org/10.1021/bi00501a016· OSTI ID:5530099
; ;  [1];  [2]
  1. Institut Curie-Biologie, Orsay (France)
  2. Univ. Rene-Descartes, Paris (France)

Disulfide bond reduction by the CO{sub 2}{sup {center dot}{minus}} radical was investigated in aponeocarzinostatin, aporiboflavin-binding protein, and bovine immunoglobulin. Protein-bound cysteine free thiols were formed under {gamma}-ray irradiation in the course of a pH-dependent and protein concentration dependent chain reaction. The chain efficiency increased upon acidification of the medium, with an apparent pK{sub a} around 5, and decreased abruptly below pH 3.6. It decreased also at neutral pH as cysteine accumulated. From pulse radiolysis analysis, CO{sub 2}{sup {center dot}{minus}} proved able to induce rapid one-electron oxidation of thiols and of tyrosine phenolic groups in addition to one-electron donation to exposed disulfide bonds. The bulk rate constant of CO{sub 2}{sup {center dot}{minus}} uptake by the native proteins was 5{minus} to 10-fold faster at pH 3 than at pH 8, and the protonated form of the disulfide radical anion, appeared to be the major protein radical species formed under acidic conditions. Formation of the disulfide radical cation, phenoxyl radical Tyr-O{sup {center dot}} disproportionation, and phenoxyl radical induced oxidation of preformed thiol groups should also be taken into consideration to explain the fate of the oxygen-centered phenoxyl radical.

OSTI ID:
5530099
Journal Information:
Biochemistry; (USA), Vol. 29:49, Issue 49; ISSN 0006-2960
Country of Publication:
United States
Language:
English