Protein sulphur functions can host a single electron on sulphur atoms in redox processes linking thiols to disulphides. However, experimental results have shown that the single electron can also reside on carbon atoms leading to protein damage. We have investigated this possibility on cystine for two initial conformations. The other site of electron fixation is always the carbonyl function. When there is no carbonyl, the electron remains on the sulphur atoms. In a model of the active site of thioredoxin (cystine, the carboxylic group of aspartic acid 30 and a water molecule), only the carbonyl group of the cystine is reactive.
Research on Chemical Intermediates – Springer Journals
Published: Jun 23, 2009
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