Simultaneous reduction and mercuration of disulfide bonds by monovalent mercury

M. M. David*, R. Sperling, I. Z. Steinberg

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

Mercurous acetate was found to simultaneously reduce and mercurate disulfide bonds according to the following scheme: {A figure is presented} The reaction was studied on low molecular weight disulfide compounds by means of ultraviolet and CD spectroscopy. An intermediate complex is formed involving mercury associated with the disulfide compound, probably by binding to a vicinal amino or amido group. In the case of cystine, decomposition of the intermediate complex follows first-order kinetics with a half-life of 25 min (25 °C). Reaction of ribonuclease with monovalent mercury was found to result in the reduction and mercuration of some of the disulfide bonds of the protein molecule.

Original languageEnglish
Pages (from-to)101-111
Number of pages11
JournalBBA - Protein Structure
Volume359
Issue number1
DOIs
StatePublished - 7 Jul 1974
Externally publishedYes

Fingerprint

Dive into the research topics of 'Simultaneous reduction and mercuration of disulfide bonds by monovalent mercury'. Together they form a unique fingerprint.

Cite this