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 language | English |
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Pages (from-to) | 101-111 |
Number of pages | 11 |
Journal | BBA - Protein Structure |
Volume | 359 |
Issue number | 1 |
DOIs | |
State | Published - 7 Jul 1974 |
Externally published | Yes |