Metal-mediated reactions modeled after nature

The Collaborative Research Center (CRC) 436 'Metal-Mediated Reactions Modeled after Nature' was founded for the express purpose of analyzing the catalytic principles of metallo-enzymes in order to construct efficient catalysts on a chemical basis. The structure of the active center and nei...

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Bibliographic Details
Published in:Journal of biotechnology 2002-04, Vol.90 (2), p.73-94
Main Authors: Diekmann, Stephan, Weston, Jennie, Anders, Ernst, Boland, Wilhelm, Schönecker, Bruno, Hettmann, Thomas, von Langen, Johannes, Erhardt, Stefan, Mauksch, Michael, Bräuer, Michael, Beckmann, Christoph, Rost, Matthias, Sperling, Petra, Heinz, Ernst
Format: Article
Language:English
Subjects:
Animals
Catalysis
Cattle
Enzymes - chemical synthesis
Enzymes - metabolism
Metals - chemistry
Metals - metabolism
Models, Chemical
Models, Molecular
Molecular Conformation
Molecular Mimicry
Molecular Structure
Stereoisomerism
Structure-Activity Relationship
Substrate Specificity
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Summary:The Collaborative Research Center (CRC) 436 'Metal-Mediated Reactions Modeled after Nature' was founded for the express purpose of analyzing the catalytic principles of metallo-enzymes in order to construct efficient catalysts on a chemical basis. The structure of the active center and neighboring chemical environment in enzymes serves as a focal point for developing reactivity models for the chemical redesign of catalysts. Instead of simply copying enzyme construction, we strive to achieve new chemical intuition based on the results of long-lasting natural evolution. We hope for success, since nature uses a limited set of building blocks, whereas we can apply the full repertoire of chemistry. Key substrates in this approach are small molecules, such as CO2, O2 NO3- and N2. Nature complexes these substrates, activates them and performs chemical transformations--all within the active center of a metalloenzyme. In this article, we report on some aspects and first results of the Collaborative Research Center (CRC) 436, such as nitrate reductase, sphingolipid desaturase, carbonic anhydrase, leucine aminopeptidase and dopamine beta-monooxygenase.
ISSN:0168-1656