Characterising and exploiting hydrogen tunnelling in environmentally and medically important enzymes

Enzymes are remarkable catalysts that can increase reaction rates by up to 19 orders of magnitude. There is presently debate as to whether some enzymes derive part of their catalytic power from quantum-tunnelling - the process by which some reactions, such as hydrogen transfer, can occur by tunnelling through, rather than passing over, an activation energy barrier. We will use a range of cutting-edge kinetic, structural and theoretical approaches to study the contribution of tunnelling to reactions catalysed by two important enzymes: a reductase found in pathogenic and methane-producing bacteria and the first computationally designed enzyme, a kemp eliminase. Our findings will be used to advance protein and drug design strategies.