Authors: Sam Hay Nigel S Scrutton
Publish Date: 2008/09/03
Volume: 98, Issue: 1-3, Pages: 169-
Abstract
Over the last 10 years studies of enzyme systems have demonstrated that in many cases Htransfers occur by a quantum mechanical tunneling mechanism analogous to longrange electron transfer Htransfer reactions can be described by an extension of Marcus theory and by substituting hydrogen with deuterium or even tritium it is possible to explore this theory in new ways by employing kinetic isotope effects Because hydrogen has a relatively short deBroglie wavelength Htransfers are controlled by the width of the reaction barrier By coupling protein dynamics to the reaction coordinate enzymes have the potential ability to facilitate more efficient Htunneling by modulating barrier properties In this review we describe recent advances in both experimental and theoretical studies of enzymatic Htransfer in particular the role of protein dynamics or promoting motions We then discuss possible consequences with regard to tyrosine oxidation/reduction kinetics in Photosystem II
Keywords: