Abstract
The mechanochemistry of the disulfide bridge--that is, the influence of an externally applied force on the reactivity of the sulfur-sulfur bond--is investigated by unrestricted Kohn-Sham theory. Specifically, we apply the COGEF (constrained geometry simulates external force) approach to characterize the mechanochemistry of the disulfide bond in three different chemical environments: dimethyl disulfide, cystine, and a 102-atom model of the I27 domain in the titin protein. Furthermore, the mechanism of the thiol-disulfide reduction reaction under the effect of an external force is investigated by considering the COGEF potential for the adduct and transition-state clusters. With the unrestricted Becke-three-parameter-Lee-Yang-Parr (UB3LYP) exchange-correlation functional in the 6-311++G(3df,3pd) orbital basis, the rupture force of dimethyl disulfide is 3.8 nN at a disulfide bond elongation of 35 pm. The interaction with neighboring groups and the effect of conformational rigidity of the protein environment have little influence on the mechanochemical characteristics. Upon stretching, we make the following observations: the diradical character of the disulfide bridge increases; the energy difference between the singlet ground state and low-lying triplet state decreases; and the disulfide reduction is promoted by an external force in the range 0.1-0.4 nN. Our model of the interplay between force and reaction mechanism is in qualitative agreement with experimental observations.
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