Dr. rer. nat. Matthias Stein, M.Sc.
Dr. rer. nat. Matthias Stein, M.Sc.
Phone: +49 391 6110 436
Fax: +49 391 6110 403



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Chiral Recognition

Chiral molecules differ in the stereochemistry of ONE atom (stereocentre). The two forms of the entity may have identical physical properties but behave differently under physiological conditions. The separation of chiral forms of a molecule (enantiomers) is thus of fundamental importance to the chemical and pharmaceutical idustry.

We investigate the separation of enantiomers by

  • liquid phase extraction
  • formation of diastereomeric complexes
  • enantioselective crystallization.

The detailed understanding of the behaviour of chiral molecules in different phases requires an accurate description of the respective binding affinities and solute-solvent interactions. It is our aim to rationalize processes that lead to enantiopure entities and design specific receptors.

Molecular Systems Biology

In systems biology, the focus of attention shifts from investigating single proteins in detail to protein complex formation, proteins in pathways and the regulation of proteins in networks.
We still characterize proteins and protein behaviour at the molecular level but with a larger scope. Our research is on comparative enzymology. We are looking at the same enzyme/protein in different species, proteins in networks and protein-protein communication. We are involved in the development of approaches to calculate enzymatic kinetic parameters which may enter kinetic models.
Areas of interest are

  • metabolic and signalling networks
  • posttranslational modifications of proteins
  • dynamics of proteins and rates of association.


The availability of genome-wide amino acid sequences offers the possibility to gain additional insight into protein family evolution and biological process design.
We make use of tools of bioinformatics to investigate protein functional domain conservation and evolution, perform large scale comparative protein structural modelling and analyze the variation of protein surface properties across species or along physiological pathways.

Bioinorganic Chemistry

The structure-to-function relationship in catalytically active complexes is not always clear. Nature uses the variability of nature of metal atom, ligands and coordination geometry to perform and optimize the turnover of a large number of chemical reactions.
With the use of computational chemistry approaches, biological, bioinorganic or biomimetic complexes can be structurally characterized, reactive intermediates identified and reaction mechanisms elucidated.
Design principles from nature can be illuminated and converted into functional biomimetic systems. Particular emphasis is placed on the calculation of data accessible from spectroscopy, i.e. NMR, EPR, UV/Vis, IR and Raman.

Hydrogen Conversion

[FeFe]-hydrogenases possess a complicated active site with six iron atoms to perform the reaction. The challenge is to design simpler (e.g. mononuclear) cheap catalysts with the same functionality. Zoom Image
[FeFe]-hydrogenases possess a complicated active site with six iron atoms to perform the reaction. The challenge is to design simpler (e.g. mononuclear) cheap catalysts with the same functionality. [less]

There are microorganisms which catalyze the conversion of molecular hydrogen. According to the transition metal of their active sites, they have been classified as [NiFe]-, [FeFe]- or [Fe] hydrogenases.

The detailed investigation of the reaction mechanisms of these enzymes will lead to

  • understanding of nature's design principles
  • transformation of insight into biomimetic systems
  • design and development of hydrogen fuel cells.

Current research areas are

  • characterization of oxygen-tolerant hydrogenases
  • combination of photosynthesis and hydrogenase for light-driven hydrogen production
  • investigation of alternative hydrogen generating enzymes.
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