Faculty of Chemistry

New publications and Deans

Recent Publications

by Marvin Oßkopp, Armin Löwe, Carlos M.S. Lobo, Sebastian Baranyai, Thulile Khoza, Michael Auinger and Elias Klemm

Journal of CO2 Utilization

For further information please contact:
Prof. Elias Klemm
Institute of Technical Chemistry
University of Stuttgart

by Ramananda Maity and Biprajit Sarkar

 

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

by J. Karst, M. Floess, M. Ubl, C. Dingler, C. Malacrida, T. Steinle, S. Ludwigs,
M. Hentschel, und H. Giessen

Science 2021, 374, 6567, 612

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

by Pit Boden, Patrick Di Martino-Fumo, Tobias Bens, Sophie Steiger, Uta Albold, Gereon Niedner-Schatteburg, Markus Gerhards and Biprajit Sarkar

Chem. Eur. J. 2021, 27, 12959 –12964 

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

by Felix Ziegler, Hamzeh Kraus, Mathis J. Benedikter, Dongren Wang, Johanna R. Bruckner, Michal Nowakowski, Kilian Weißer, Helena Solodenko, Guido Schmitz, Matthias Bauer, Niels Hansen, and Michael R. Buchmeiser

ACS Catal. 2021, 11, 11570−11578

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

by Saravanakumar Murugan, Stefan Niesen, Julian Kappler, Kathrin Küster, Ulrich Starke, and Michael R. Buchmeiser

Batteries & Supercaps 2021, 4, 1636–1646

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

by Biswarup Jash, Peter Tremmel, Dejana Jovanovic and Clemens Richert

Read also the comments of other researchers.

A brief explanation: The Molecules that were Able to Start Translation

Nature Chemistry

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

by Sabrina Henche, Bettina M. Nestl and Bernhard Hauer

Efficiency and selectivity in forming carbon-carbon bonds determine chemical manufacturing and are crucial for a sustainable society. The Friedel-Crafts (FC) alkylation represents one of the oldest carbon-carbon bond formation reactions and enables the pairing of aromatics and aliphatics. Despite its age and comprehension, FC reactions often suffer from poor selectivity, follow-up reactions, and ultimately low atom economy. Using the Brønsted acid squalene-hopene cyclase from Alicyclobacillus acidocaldarius we have set the stage for highly atom economical and regio- and product selective FC alkylations. Owing to its relaxed substrate specificity, we demonstrated the intramolecular FC alkylation of an unbiased geranyl phenyl ether. Furthermore, screening a mutant library and compared orthologs to gain complete control over product selectivity and increased activity. Molecular docking studies have been performed to gain more insights into these findings. Thus, the applicability of this enzymatic Brønsted acid will facilitate converting more diverse substrates and implementing intermolecular reactions in the future. 

ChemCatChem, DOI: 10.1002/cctc.202100452

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

by Andreas Schneider, Philipp Jegl, and Bernhard Hauer

It is of rising interest to expand an enzyme’s reaction portfolio beyond its physiological scope. In this endeavor, two challenges are of particular interest: Detailed understanding of the enzyme’s structure-function relationship as well as profound comprehension of the catalyzed chemical reaction pathways. Prerequisite in this task is the identification and variation of catalytic core elements, e.g. access, orientation and anchoring of a substrate via electronic interaction in tunnels or active site. In this paper we focused our engineering efforts on molecular anchors and highlighted the ability of hydrogen-bond mediated direction of cationic cascades in terpene cyclases. As a result, the engineered cyclase provides efficient access to value-added apocarotenoids by cutting down synthetic routes to a single step with unprecedented selectivity and high yields.

Angew. Chem. Int. Ed. 2021, 60

Highlight in Nature Catalysis:
Völler, JS. Directed cationic cascades Nat. Catal. 4, 262 (2021)

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

by Julian L. Wissner, Jona T. Schelle, Wendy Escobedo-Hinojosa, Andreas Vogel, and Bernhard Hauer

Rieske non-heme iron dioxygenases are fascinating enzymes, which are able to oxyfunctionalize aromatic compounds via a dearomatizing cis-dihydroxylation reaction. The generated valuable cis-diols find numerous applications in synthetic organic chemistry, primary as synthons for pharmaceuticals. By semi-rational evolution, we lighted up the toluene dioxygenase (TDO) capability to convert bulkier compounds at unprecedented reported conversions. Here, we provide a set of novel TDO-based biocatalysts useful for the preparation of oxyfunctionalized bicyclic scaffolds, which are valuable to perform downstream synthetic processes.

Adv. Synth. Catal. 2021, 363

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

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

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