Parallel modeling of both enzyme active sites and biomimetic complexes provides closer coupling of these two areas and a better understanding of their similarities and differences. Our recent computational work has developed along several lines: (1) thermodynamic properties such as acidity constants (pKa) and redox potentials (E0) of both enzyme active sites and model complexes, (2) explorations of the mechanism and thermodynamics of reactions that produce oxygenated complexes, (3) electronic structure and rearrangement mechanisms of oxidized, reduced, and protonated complexes and active sites,  (4) correlation of IR frequencies as a means of identifying the structure and state of active sites, and (5) the electronic structure of new diiron nitrosyl complexes, where replacement of CO by NO+ in some way parallels the effect of oxidizing the diiron complex.

Computational modeling of hydrogenases and their biomimetics

248th National Meeting (2014)

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