We are grateful to Matthias Lee for developing the enzymatic assay, to Claudia Baier for recording cyclic voltammograms and to the staff of PXII at the Swiss Light Source (Villigen), in particular Clemens Schulze-Briese, for help during data collection. We thank the Hans-Fischer Gesellschaft and the Stifterverband für die Deutsche Wissenschaft (Projekt-Nr. 11047: Forschungsdozentur Molekulare Katalyse) for financial support.
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Communication
Structure of Active IspH Enzyme from Escherichia coli Provides Mechanistic Insights into Substrate Reduction†
Article first published online: 30 JUN 2009
DOI: 10.1002/anie.200900548
Copyright © 2009 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Additional Information
How to Cite
Gräwert, T., Rohdich, F., Span, I., Bacher, A., Eisenreich, W., Eppinger, J. and Groll, M. (2009), Structure of Active IspH Enzyme from Escherichia coli Provides Mechanistic Insights into Substrate Reduction. Angewandte Chemie International Edition, 48: 5756–5759. doi: 10.1002/anie.200900548
- †
Publication History
- Issue published online: 15 JUL 2009
- Article first published online: 30 JUN 2009
- Manuscript Revised: 25 MAR 2009
- Manuscript Received: 29 JAN 2009
Funded by
- Hans-Fischer Gesellschaft
- Stifterverband für die Deutsche Wissenschaft
Keywords:
- iron–sulfur clusters;
- enzymes;
- isoprenes;
- non-mevalonate pathway;
- reaction mechanisms
Graphical Abstract
The terminal step of the non-mevalonate pathway of terpene biosynthesis is catalyzed by IspH (see scheme). In the crystal structure of IspH from E. coli, a bound inorganic diphosphate ligand occupies the position of the diphosphate residue of the substrate. Together with mutation studies and theoretical calculations, these data support a mechanism which is analogous to the Birch reduction of allylic alcohols.