Ivana Franke

 

Schering Preis 2001

Dr. Matthias Stein

anterio consult & research GmbH, Mannheim

The reaction mechanism of biological hydrogen conversion

During his Ph.D. thesis, Matthias Stein worked on the elucidation of the reaction mechanism of biological hydrogen conversion by enzymes called hydrogenases.

Hydrogenases exist in the oldest bacteria on earth and have adapted to living under volcanic conditions. The hydrogenases from the bacteria Desulfovibrio respire sulphur compounds and use molecular hydrogen as a source of energy for driving their metabolism. Most interesting, they catalyse the reversible heterolytic dissociation of molecular hydrogen. This qualifies them as candidate for the biological delivery of hydrogen as a non-fossil energy carrier for i.e. fuel cells in automobiles.

The [NiFe] hydrogenases possess an unusual heterobimetallic active site where the reaction occurs. The protein structure of the investigated enzymes has recently been determined but only provides a static picture and does not reveal details of the reaction mechanism.

Protein preparations in frozen solution and in single crystals were investigated by various techniques of Electron Spin Resonance (ESR) spectroscopy and electron-nuclear double resonance (ENDOR) experiments. One could thus obtain a detailed insight into the electronic structure and ligand binding situation of the enzyme's catalytic site in several intermediate steps. Furthermore, using modern relativistic Density Functional Theory (DFT) calculations, it was possible to accurately calculate the spectroscopic observables and compare them with those measured experimentally. For the first time it was feasible to treat systems as complicated and big as that of an enzymatic active centre.

Thus, a direct structure-to-function relationship for the active centre during the catalytic process could be established and revealed the atomic composition of the active centre in every step, the substrate binding site and the reaction mechanism. The fine-tuning of the reaction mechanism by the protein environment and the protein cofactors was also investigated and showed nature's sophistication in constructing natural catalysts.

The project was performed at the Max Volmer Laboratory for Biophysical Chemistry at the Technical University Berlin under the supervision of Prof. Wolfgang Lubitz. The international and interdisciplinary project involved research groups from Europe and Japan and was a co-operation between protein structural chemists, microbiologists, physicists, spectroscopists and theoretical chemists. The project was supported by the Fonds der Chemischen Industrie and the Deutsche Forschungsgemeinschaft (DFG). Matthias Stein is now working with the anterio consult & research GmbH, Mannheim, on computer-aided drug design and all aspects of scientific computing.

2001_Stein_grau

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