Janosch Gröning

Müller, Erik; Sosedov, Olga; Gröning, Janosch Alexander David; Stolz, Andreas (2021): Synthesis of (R)-mandelic acid and (R)-mandelic acid amide by recombinant E. coli strains expressing a (R)-specific oxynitrilase and an arylacetonitrilase. In: Biotechnology letters 43 (1), S. 287–296. DOI: 10.1007/s10529-020-02998-8.

Nething, Christoph; Smirnova, Maya; Gröning, Janosch A.D.; Haase, Walter; Stolz, Andreas; Sobek, Werner (2020): A method for 3D printing bio-cemented spatial structures using sand and urease active calcium carbonate powder. In: Materials & Design 195, S. 109032. DOI: 10.1016/j.matdes.2020.109032.

Willrodt, Christian; Gröning, Janosch A. D.; Nerke, Philipp; Koch, Rainhard; Scholtissek, Anika; Heine, Thomas et al. (2020): Highly Efficient Access to (S )‐Sulfoxides Utilizing a Promiscuous Flavoprotein Monooxygenase in a Whole‐Cell Biocatalyst Format. In: ChemCatChem 12 (18), S. 4664–4671. DOI: 10.1002/cctc.201901894.

Aleshintsev, Aleksey; Eppinger, Erik; Gröning, Janosch A. D.; Stolz, Andreas; Gupta, Rupal (2019): Substrate promiscuity and active site differences in gentisate 1,2-dioxygenases: electron paramagnetic resonance study. In: Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry 24 (2), S. 287–296. DOI: 10.1007/s00775-019-01646-5.

Brunner, Siegfried; Eppinger, Erik; Fischer, Stefanie; Gröning, Janosch; Stolz, Andreas (2018): Conversion of aliphatic nitriles by the arylacetonitrilase from Pseudomonas fluorescens EBC191. In: World journal of microbiology & biotechnology 34 (7), S. 91. DOI: 10.1007/s11274-018-2477-9.

Retamal-Morales, Gerardo; Heine, Thomas; Tischler, Judith S.; Erler, Beate; Gröning, Janosch A. D.; Kaschabek, Stefan R. et al. (2018): Draft genome sequence of Rhodococcus erythropolis B7g, a biosurfactant producing actinobacterium. In: Journal of biotechnology 280, S. 38–41. DOI: 10.1016/j.jbiotec.2018.06.001.

Westphal, Adrie H.; Tischler, Dirk; Heinke, Florian; Hofmann, Sarah; Gröning, Janosch A. D.; Labudde, Dirk; van Berkel, Willem J. H. (2018): Pyridine Nucleotide Coenzyme Specificity of p-Hydroxybenzoate Hydroxylase and Related Flavoprotein Monooxygenases. In: Frontiers in microbiology 9, S. 3050. DOI: 10.3389/fmicb.2018.03050.

Haferburg, Götz; Gröning, Janosch A. D.; Schmidt, Nadja; Kummer, Nicolai-Alexeji; Erquicia, Juan Carlos; Schlömann, Michael (2017): Microbial diversity of the hypersaline and lithium-rich Salar de Uyuni, Bolivia. In: Microbiological research 199, S. 19–28. DOI: 10.1016/j.micres.2017.02.007.

Gröning, Janosch A. D.; Eulberg, Dirk; Tischler, Dirk; Kaschabek, Stefan R.; Schlömann, Michael (2014): Gene redundancy of two-component (chloro)phenol hydroxylases in Rhodococcus opacus 1CP. In: FEMS microbiology letters 361 (1), S. 68–75. DOI: 10.1111/1574-6968.12616.

Gröning, Janosch A. D.; Kaschabek, Stefan R.; Schlömann, Michael; Tischler, Dirk (2014): A mechanistic study on SMOB-ADP1: an NADH:flavin oxidoreductase of the two-component styrene monooxygenase of Acinetobacter baylyi ADP1. In: Archives of microbiology 196 (12), S. 829–845. DOI: 10.1007/s00203-014-1022-y.

Roth, Christian; Gröning, Janosch Alexander D.; Kaschabek, Stefan Rudolf; Schlömann, Michael; Sträter, Norbert (2013): Crystal structure and catalytic mechanism of chloromuconolactone dehalogenase ClcF from Rhodococcus opacus 1CP. In: Molecular microbiology 88 (2), S. 254–267. DOI: 10.1111/mmi.12182.

Gröning, Janosch A. D.; Roth, Christian; Kaschabek, Stefan R.; Sträter, Norbert; Schlömann, Michael (2012): Recombinant expression of a unique chloromuconolactone dehalogenase ClcF from Rhodococcus opacus 1CP and identification of catalytically relevant residues by mutational analysis. In: Archives of biochemistry and biophysics 526 (1), S. 69–77. DOI: 10.1016/j.abb.2012.07.007.

Oelschlägel, Michel; Gröning, Janosch A. D.; Tischler, Dirk; Kaschabek, Stefan R.; Schlömann, Michael (2012): Styrene oxide isomerase of Rhodococcus opacus 1CP, a highly stable and considerably active enzyme. In: Applied and environmental microbiology 78 (12), S. 4330–4337. DOI: 10.1128/AEM.07641-11.

Roth, Christian; Kaschabek, Stefan R.; Gröning, Janosch A. D.; Handrek, Thomas; Schlömann, Michael; Sträter, Norbert (2012): Crystallization and preliminary characterization of chloromuconolactone dehalogenase from Rhodococcus opacus 1CP. In: Acta crystallographica. Section F, Structural biology and crystallization communications 68 (Pt 5), S. 591–595. DOI: 10.1107/S1744309112011888.

Tischler, Dirk; Gröning, Janosch A. D.; Kaschabek, Stefan R.; Schlömann, Michael (2012): One-component styrene monooxygenases: an evolutionary view on a rare class of flavoproteins. In: Applied biochemistry and biotechnology 167 (5), S. 931–944. DOI: 10.1007/s12010-012-9659-y.

Gröning, Janosch A. D.; Tischler, Dirk; Kaschabek, Stefan R.; Schlömann, Michael (2010): Optimization of a genome-walking method to suit GC-rich template DNA from biotechnological relevant Actinobacteria. In: Journal of basic microbiology 50 (5), S. 499–502. DOI: 10.1002/jobm.201000032.

Tischler, Dirk; Kermer, René; Gröning, Janosch A. D.; Kaschabek, Stefan R.; van Berkel, Willem J. H.; Schlömann, Michael (2010): StyA1 and StyA2B from Rhodococcus opacus 1CP: a multifunctional styrene monooxygenase system. In: Journal of bacteriology 192 (19), S. 5220–5227. DOI: 10.1128/jb.00723-10.

Gröning, Janosch; Held, Claudia; Garten, Claudia; Claussnitzer, Ute; Kaschabek, Stefan R.; Schlömann, Michael (2007): Transformation of diclofenac by the indigenous microflora of river sediments and identification of a major intermediate. In: Chemosphere 69 (4), S. 509–516. DOI: 10.1016/j.chemosphere.2007.03.037.

Thiel, Monika; Kaschabek, Stefan R.; Gröning, Janosch; Mau, Margit; Schlömann, Michael (2005): Two unusual chlorocatechol catabolic gene clusters in Sphingomonas sp. TFD44. In: Archives of microbiology 183 (2), S. 80–94. DOI: 10.1007/s00203-004-0748-3.

König, Christina; Eulberg, Dirk; Gröning, Janosch; Lakner, Silvia; Seibert, Volker; Kaschabek, Stefan R.; Schlömann, Michael (2004): A linear megaplasmid, p1CP, carrying the genes for chlorocatechol catabolism of Rhodococcus opacus 1CP. In: Microbiology (Reading, England) 150 (Pt 9), S. 3075–3087. DOI: 10.1099/mic.0.27217-0.

Moiseeva, Olga V.; Solyanikova, Inna P.; Kaschabek, Stefan R.; Gröning, Janosch; Thiel, Monika; Golovleva, Ludmila A.; Schlömann, Michael (2002): A new modified ortho cleavage pathway of 3-chlorocatechol degradation by Rhodococcus opacus 1CP: genetic and biochemical evidence. In: Journal of bacteriology 184 (19), S. 5282–5292. DOI: 10.1128/jb.184.19.5282-5292.2002.

Vollmer, M. D.; Hoier, H.; Hecht, H. J.; Schell, U.; Gröning, J.; Goldman, A.; Schlömann, M. (1998): Substrate specificity of and product formation by muconate cycloisomerases: an analysis of wild-type enzymes and engineered variants. In: Applied and environmental microbiology 64 (9), S. 3290–3299. DOI: 10.1128/AEM.64.9.3290-3299.1998.