Rita and John Cornforth Award 2009 winner

Awarded for their pioneering studies in quantum enzymology, combining high resolution time-resolved structural analysis, computational chemistry and numerical modelling and theory with reaction kinetics in a multidisciplinary chemical biology approach.

About the winners

The effectiveness of cutting-edge research is dependent upon the ability of the scientific community to self-assemble into multidisciplinary teams to tackle effectively large, complicated problems.

We have "self-assembled" a world-leading research team with an extensive and complementary skill base. This is underpinned by the development of cutting-edge experimental and theoretical approaches, and has involved a strong interplay between high resolution/time-resolved structural analysis, detailed computational chemistry and numerical modelling and theory, fast reaction kinetics and chemical biology.

Our studies have provided new and deep insight and understanding of the new field of 'quantum enzymology'. This has taken place over a period of ~10 years, initially against a resistant community, has challenged conventional 'mainstream' thinking in the field and pushed new boundaries in our physical understanding of enzyme catalysis.

The text-book description of catalysis states that enzymes reduce the energy required to surmount the barrier, which leads to enhanced rates. This classical over-the-barrier treatment, known as transition state theory, has been used to depict enzyme-catalysed reactions over the last 50 years.

Over the last decade, we (and others) have shown that quantum mechanical principles - in particular hydrogen tunnelling - could be used to rationalise the temperature, and latterly pressure, behaviour of isotope effects in enzyme-catalysed H-transfer reactions. Quantum enzymology will impact widely on both fundamental and applied work with enzyme systems.