Faculty of Chemistry

New publications and Deans

Recent Publications

by Jessica Stubbe, Simon Suhr, Julia Beerhues, Maite Nößler and Biprajit Sarkar

Chem. Sci.,2021,12,3170–3178

For further information please contact:
Prof. Biprajit Sarkar
Institute of Inorganic Chemistry
University of Stuttgart

by Lea R. Rapp, Sérgio M. Marques, Erna Zukic, Benjamin Rowlinson, Mahima Sharma, Gideon Grogan, Jiri Damborsky & Bernhard Hauer

In a recent paper, we have shown that variations in tunnel geometry affect the specificity of biological oxidations, leading to increased activity and altered selectivity, as well as an expanded substrate scope. In this paper, we study the second main strategy that can confer specificity to the orientation and anchoring of a substrate. Through molecular modeling and MD simulations, we gained deeper insights into enzyme dynamics and demonstrated that anchoring of the substrate and reducing the protein scaffold flexibility is a critical factor for increased efficiency of this enzyme towards the terminal hydroxylation of octanoic acid.

ACS Catalysis (2021), 11, 3182 - 3189

For further information please contact:
Prof. Bernhard Hauer
Institute of Biochemistry and Technical Biochemistry,
Department Technical Biochemistry
University of Stuttgart

by Peter M. Heinemann, Daniel Armbruster & Bernhard Hauer 

Rieske non-haem dioxygenases are enzymes achieving selective oxidation of substrates. Nature has two different strategies to achieve this selectivity either by size and shape or substrate orientation. Part of this specificity arises from a sieve - like structure called tunnel that hampers the access of certain molecules to the active site of an enzyme. These tunnels are formed by loop-like structures. In our paper we have been introducing or deleting several amino acids residues to modulate these loops. However, the active site as well as the core of the protein structure is untouched. These drastic modifications emulate the specificity of biological oxidations and result in increased activity and altered selectivity as well as a broadening substrate scope. First analysis of these enzyme variants points towards an altered tunnel geometry and chemists might find inspiration in designing catalysts.

Nature Communications Volume 12, Article Number: 1095 (2021) 

For further information please contact:
Prof. Bernhard Hauer
Institute of Biochemistry and Technical Biochemistry,
Department Technical Biochemistry
University of Stuttgart

Novel molecular anions found in ternary germanium nitride crystals give a clue on similarities and differences of chemistry of germanium nitrides and the technologically immensely important silicon nitrides. The research article reports on the synthesis and properties of the first germanium(III) nitrides featuring hitherto unknown [Ge2N6]12– anions, virtually unknown for the well studied nitridosilicates. Grown under an inert gas atmosphere, these compounds exemplify the tremendous flexibility of nitridogermanates in terms of chemical bonding and accessible oxidation states.

by L. Link, M. Pathak, Dr. F. Jach, Dr. P. Koželj, Dr. A. Ormeci, Dr. P. Höhn and Prof. Dr. R. Niewa

Angew. Chemie, 2021,60, 2-7

For further information please contact:
Prof. Rainer Niewa
Institute of Inorganic Chemistry
University of Stuttgart

by Erna Davydova, Tadahiro Shimazu, Maren Kirstin Schuhmacher, Magnus E. Jakobsson, Hanneke L. D. M. Willemen, Tongri Liu, Anders Moen, Angela Y. Y. Ho, Jędrzej Małecki, Lisa Schroer, Rita Pinto, Takehiro Suzuki, Ida A. Grønsberg, Yoshihiro Sohtome, Mai Akakabe, Sara Weirich, Masaki Kikuchi, Jesper V. Olsen, Naoshi Dohmae, Takashi Umehara, Mikiko Sodeoka, Valentina Siino, Michael A. McDonough, Niels Eijkelkamp, Christopher J. Schofield, Albert Jeltsch, Yoichi Shinkai and Pål Ø. Falnes

In this work, the group of Prof. Jeltsch explored post-translational methylation of proteins which plays a crucial role in regulating various aspects of the function of proteins. Histidine methylation is a relatively rare and understudied protein modification. In this work, Prof. Jeltsch et al. investigated the METTL9 protein and showed that it represents a novel protein histidine methylation. The enzyme has a preference for methylation of the first histidine in HXH sequences, where X should be a small amino acid residue (preferentially A, N, G, S or T). Based on this, several cellular peptide and proteins substrates of METTL9 were discovered. Overall, METTL9 mediates the formation of the majority of 1-methylhistidine present in mouse and human proteomes including methylation of the NDUFB3 subunit of mitochondrial respiratory complex I, which was shown to enhance aerobic respiration.

Nature Communications Vol. 12, Article number: 891 (2021)

For further information please contact:
Prof. Albert Jeltsch
Institute of Biochemistry and Technical Biochemistry,
Biochemistry Department
University of Stuttgart

by Carsten Dingler, Henry Müller, Matthias Wieland, Dominik Fauser,
Holger Steeb and Sabine Ludwigs

Avd. Mat. 2021

For further information please contact:
Prof. Sabine Ludwigs
Institute of Polymer Chemistry
University of Stuttgart

by Ludwig L. Bengel, Benjamin Aberle, Alexander-N. Egler-Kemmerer, Samuel Kienzle, Bernhard Hauer and Stephan C. Hammer

Selective alkylation of pyrazoles could solve a challenge in chemistry and streamline synthesis of important molecules. A pyrazole-methylating enzyme family that transfers alkyl groups in catalyst-controlled highly selective C-N bond formations to the pyrazole substrate was created using a computational enzyme library design tool. A second, promiscuous enzyme generates non-natural-analogues of the common cofactor S-adenosyl-l-methionine utilizing simple haloalkanes as precursors. These enzymes were combined in a bienzymatic cascade where the cofactor is recycled and only used in catalytic amounts. With this enzymatic system, selective pyrazole alkylation (methylation, ethylation and propylation) was achieved with unprecedented regioselectivities (>99%), regiodivergence and in a first example on preparative scale.

Angew. Chem. Int. Ed., doi.org/10.1002/anie.202014239

For further information please contact:
Prof. Bernhard Hauer
Institute of Biochemistry and Technical Biochemistry,
Department Technical Biochemistry
University of Stuttgart

by Jessica Stubbe, Nicolás.Neuman, Ross McLellan, Michael G. Sommer, Maite Nößler, Julia Beerhues, Robert E. Mulvey and Biprajit Sarkar

Angew.Chem. Int. Ed. 2021, 60,499 –506, doi.org/10.1002/anie.202013376

For further information please contact:
Prof. Biprajit Sarkar
Institute of Inorganic Chemistry
University of Stuttgart

by Mithilesh Kumar Nayak, Simon Suhr, Nicolas Chrysochos, Hemant Rawat, Carola Schulzke, Vadapalli Chandrasekhar, Biprajit Sarkar and Anukul Jana

Chem. Comm. 2021, DOI: 10.1039/d0cc07385g

For further information please contact:
Prof. Biprajit Sarkar
Institute of Inorganic Chemistry
University of Stuttgart

by Mathis J. Benedikter, Janis V. Musso, Wolfgang Frey, Roman Schowner, and
Michael R. Buchmeiser

Angew. Chem. Int. Ed. 2021, 60, 1374–1382

For further information please contact:
Prof. Michael R. Buchmeiser
Institute of Polymer Chemistry
University of Stuttgart

by Mathis Benedikter, Janis Musso, Manoj K. Kesharwani, K. Leonard Sterz, Iris Elser, Felix Ziegler,
Felix Fischer, Bernd Plietker, Wolfgang Frey, Johannes Kästner, Mario Winkler, Joris van Slageren,
Michal Nowakowski, Matthias Bauer and Michael R. Buchmeiser

ACS Catal. 2020, 10, XXX, 14810–14823

For further information please contact:
Prof. Michael R. Buchmeiser
Institute of Polymer Chemistry
University of Stuttgart

by J. Han, C. Funk, J. Eyberg, S. Bailer and C. Richert

Chem. Biodiv. 2020, published online December 3

The Richert Group, in collaboration with the Bailer Group, publishes new C-nucleoside with antiviral activity.

For further information please contact:
Prof. Clemens Richert
Institute of Organic Chemistry
University of Stuttgart

Office of the Dean

This picture showsIsabella Waldner
Dr.

Isabella Waldner

Faculty Manager

To the top of the page