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Formation of disulphide bonds in the reaction of SH group-containing amino acids with trimethylamine N-oxide. A regulatory mechanism in proteins.
- Source :
-
FEBS letters [FEBS Lett] 1993 Nov 01; Vol. 333 (3), pp. 331-3. - Publication Year :
- 1993
-
Abstract
- Two amino acids containing SH group (cysteine and homocysteine)+trimethylamine N-oxide systems were studied by FTIR and 1H NMR spectroscopy. This study demonstrates that cysteine and homocysteine ethylesters react with trimethylamine N-oxide. Immediately after mixing, SH...ON<==>S-...H+ ON hydrogen bonds with large proton polarizability are are formed. Then a reaction proceeds resulting in the formation of corresponding disulphides. Trimethylamine N-oxide is present in biological systems. Thus, our results suggest that trimethylamine N-oxide may play a regulatory role in S-S bond formation in enzymes and other proteins.
Details
- Language :
- English
- ISSN :
- 0014-5793
- Volume :
- 333
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- FEBS letters
- Publication Type :
- Academic Journal
- Accession number :
- 8224204
- Full Text :
- https://doi.org/10.1016/0014-5793(93)80681-j