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Journal cover features human enzyme lysine research

Research into concerted hydrogen atom and electron transfer Mechanism for catalysis by lysine-specific demethylase is featured on the cover of the July 18 edition of The Journal of Physical Chemistry B. The research reflects the collaborative work of scientists in the Chemical Theory Center, including researchers in the groups of professor Jiali Gao and Donald Truhlar, and scientists in Japan.

Concerted hydrogen atom and electron transfer as catalyzed by human lysine-specific demethylase. The human enzyme lysine-specific demethylase catalyzes the concerted and synchronous transfer of a hydrogen atom and an electron from the substrate dimethylated lysine to a nitrogen of the coenzyme flavin adenine dinucleotide. The cover picture shows the enzyme with the substrate docked in the active site, prepared to undergo reaction. The free energy profile of the reaction, including the effects of more than 100 000 atoms of the enzyme, coenzyme, and solvent, was modeled with molecular dynamics calculations based on a reactive potential energy function obtained by electrostatically embedded multiconfiguration molecular mechanics with parameters determined by a density functional calculation on a gas-phase model.

Click here to access the July 18, 2013 issue. Click here to read the entire research article, which was first published online in May 2013.