Enzyme dynamics and tunneling enhanced by compression in the hydrogen abstraction catalyzed by soybean lipooxygenase-1

A fully microscopical simulation of the rate-limiting hydrogen abstraction catalyzed by soybean lipoxygenase-1 (SLO-1) was carried out and the rate constants and kinetic isotope effect (KIE) were calculated. The results show that the compression of the wild-type active site enzyme results in the huge contribution of tunneling to the rate of the hydrogen abstraction and the calculated KIE for the wild-type enzyme has an important dependence on the barrier width.