Reedijk Symposium 2012 - Guest Lecturers: Prof. Oliver Einsle & Prof. Nigel Scrutton

Published on May 29, 2012
Reedijk Symposium 2012 - Guest Lecturers: Prof. Oliver Einsle & Prof. Nigel Scrutton

On Friday October 26th 2012 the third annual Jan Reedijk LIC Symposium will be held. The main lectures of the day will be "Enzyme catalysis in relation to hydrogen and electron transfer" by invited speaker Prof. Nigel Scrutton (Manchester), and "Molecular enzymology of dinitrogen metabolism" by Prof. Oliver Einsle (Freiburg).

The complete programme can be found here.

Oliver Einsle: Molecular Enzymology of Dinitrogen Metabolism

The biogeochemical nitrogen cycle includes some of the most challenging catalyses known to biology. This is particularly the case for the making and breaking of dinitrogen (N2), a highly inert gas that due to its extraordinary stability constitutes a natural sink for 99% of all [N] cycling through the biosphere. It is generated from nitrous oxide (N2O) by copper-containing nitrous oxide reductase, and its reductive fixation to bioavailable ammonia is exclusively carried out by the enzyme system nitrogenase. Intricate metal clusters are found at the active sites of both proteins, and in spite of decades of extensive work the details of how these enzymes activate their inert substrates are not well understood. 

Nigel Scrutton: Enzyme catalysis in relation to hydrogen and electron transfer

Enzyme catalysis is essential to life. Despite over 100 years of effort, our understanding of the catalytic effect in enzymes from a quantitative perspective is poorly understood. Catalysis is linked inextricably to the geometry(s) of the enzyme-substrate complex, the chemical-physical properties of the active site and (potentially) dynamical contributions that are coupled to the reaction coordinate. Quantitative and predictive models of catalysis remain at the core of biocatalysis research. They underpin enzyme exploitation and engineering for sustainable energy and applications in industrial biotechnology and manufacture. Our ability to rationally design new bio-catalysts for manufacture, or re-profile existing enzymes, is currently compromised because we lack comprehensive, physical and predictive models from which to understand the origin of catalytic power. These models will emerge from the integration of state-of-the-art experimental and computational approaches involving reaction simulations; theory; advanced kinetic and spectroscopic methods; and time resolved/perturbation structural biology methods. Over a number of years we have investigated physical models of enzyme catalysis in studies of both hydrogen and electron transfer. In this lecture I will present recent studies in which we have used experimental, computational and theoretical approaches, at the ensemble and single molecule levels, to investigate hydrogen transfer in enzyme active sites. Our work has  shown the importance of quantum tunnelling and fast (compressive) dynamics in these reactions. I will illustrate these recent developments by reference to model enzyme systems using kinetics, spectroscopic, computational and structural biology approaches.

 

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