@article{HuckSchiffelsHerreraetal.2013, author = {Huck, Christina and Schiffels, Johannes and Herrera, Cony N. and Schelden, Maximilian and Selmer, Thorsten and Poghossian, Arshak and Baumann, Marcus and Wagner, Patrick and Sch{\"o}ning, Michael Josef}, title = {Metabolic responses of Escherichia coli upon glucose pulses captured by a capacitive field-effect sensor}, series = {Physica Status Solidi (A)}, volume = {210}, journal = {Physica Status Solidi (A)}, number = {5}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {0031-8965}, doi = {10.1002/pssa.201200900}, pages = {926 -- 931}, year = {2013}, abstract = {Living cells are complex biological systems transforming metabolites taken up from the surrounding medium. Monitoring the responses of such cells to certain substrate concentrations is a challenging task and offers possibilities to gain insight into the vitality of a community influenced by the growth environment. Cell-based sensors represent a promising platform for monitoring the metabolic activity and thus, the "welfare" of relevant organisms. In the present study, metabolic responses of the model bacterium Escherichia coli in suspension, layered onto a capacitive field-effect structure, were examined to pulses of glucose in the concentration range between 0.05 and 2 mM. It was found that acidification of the surrounding medium takes place immediately after glucose addition and follows Michaelis-Menten kinetic behavior as a function of the glucose concentration. In future, the presented setup can, therefore, be used to study substrate specificities on the enzymatic level and may as well be used to perform investigations of more complex metabolic responses. Conclusions and perspectives highlighting this system are discussed.}, language = {en} } @article{SelmerPinkenburg2008, author = {Selmer, Thorsten and Pinkenburg, Olaf}, title = {Method of cloning at least one nucleic acid molecule of interest using type IIS restriction endonucleases, and corresponding cloning vectors, kits and system using type IIS restriction endonucleases / Selmer, Thorsten ; Pinkenburg, Olaf}, year = {2008}, language = {en} } @book{Selmer1996, author = {Selmer, Thorsten}, title = {Nachweis einer neuartigen posttranslationalen Modifikation in Sulfatasen und ihr Fehlen in Enzymen aus Patienten mit multipler Sulfatase-Defizienz}, publisher = {Cuvillier}, address = {G{\"o}ttingen}, pages = {XIII, 143, IX S. : graph. Darst.}, year = {1996}, language = {de} } @article{SelmerPierikHeider2005, author = {Selmer, Thorsten and Pierik, Antonio J. and Heider, Johann}, title = {New glycyl radical enzymes catalysing key metabolic steps in anaerobic bacteria}, series = {Biological Chemistry. 386 (2005), H. 10}, journal = {Biological Chemistry. 386 (2005), H. 10}, isbn = {1431-6730}, pages = {981 -- 988}, year = {2005}, language = {en} } @article{SelmerJennemannBaueretal.1999, author = {Selmer, Thorsten and Jennemann, Richard and Bauer, Bernhard L. and Bertalanffy, Helmut}, title = {Novel glycoinositolphosphosphingolipids, basidiolipids, from Agaricus / Jennemann, Richard ; Bauer, Bernhard, L. ; Bertalanffy, Helmut ; Geyer, Rudolf ; Gschwind, Ruth, M. ; Selmer, Thorsten ; Wiegandt, Herbert}, series = {European Journal of Biochemistry. 259 (1999), H. 1-2}, journal = {European Journal of Biochemistry. 259 (1999), H. 1-2}, isbn = {0014-2956}, pages = {331 -- 338}, year = {1999}, language = {en} } @article{WernerGroebelKrumbeetal.2012, author = {Werner, Frederik and Groebel, Simone and Krumbe, Christoph and Wagner, Torsten and Selmer, Thorsten and Yoshinobu, Tatsuo and Baumann, Marcus and Sch{\"o}ning, Michael Josef}, title = {Nutrient concentration-sensitive microorganism-based biosensor}, series = {Physica Status Solidi (a)}, volume = {209}, journal = {Physica Status Solidi (a)}, number = {5}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {1862-6319}, doi = {10.1002/pssa.201100801}, pages = {900 -- 904}, year = {2012}, language = {en} } @article{PilasYaziciSelmeretal.2017, author = {Pilas, Johanna and Yazici, Yasemen and Selmer, Thorsten and Keusgen, Michael and Sch{\"o}ning, Michael Josef}, title = {Optimization of an amperometric biosensor array for simultaneous measurement of ethanol, formate, d- and l-lactate}, series = {Electrochimica Acta}, volume = {251}, journal = {Electrochimica Acta}, publisher = {Elsevier}, address = {Amsterdam}, issn = {0013-4686}, doi = {10.1016/j.electacta.2017.07.119}, pages = {256 -- 262}, year = {2017}, abstract = {The immobilization of NAD+-dependent dehydrogenases, in combination with a diaphorase, enables the facile development of multiparametric sensing devices. In this work, an amperometric biosensor array for simultaneous determination of ethanol, formate, d- and l-lactate is presented. Enzyme immobilization on platinum thin-film electrodes was realized by chemical cross-linking with glutaraldehyde. The optimization of the sensor performance was investigated with regard to enzyme loading, glutaraldehyde concentration, pH, cofactor concentration and temperature. Under optimal working conditions (potassium phosphate buffer with pH 7.5, 2.5 mmol L-1 NAD+, 2.0 mmol L-1 ferricyanide, 25 °C and 0.4\% glutaraldehyde) the linear working range and sensitivity of the four sensor elements was improved. Simultaneous and cross-talk free measurements of four different metabolic parameters were performed successfully. The reliable analytical performance of the biosensor array was demonstrated by application in a clarified sample of inoculum sludge. Thereby, a promising approach for on-site monitoring of fermentation processes is provided.}, language = {en} } @article{PilasMarianoKeusgenetal.2015, author = {Pilas, Johanna and Mariano, K. and Keusgen, M. and Selmer, Thorsten and Sch{\"o}ning, Michael Josef}, title = {Optimization of an Enzyme-based Multi-parameter Biosensor for Monitoring Biogas Processes}, series = {Procedia Engineering}, volume = {120}, journal = {Procedia Engineering}, publisher = {Elsevier}, address = {Amsterdam}, issn = {1877-7058}, doi = {10.1016/j.proeng.2015.08.702}, pages = {532 -- 535}, year = {2015}, language = {en} } @article{SelmerBuckel1999, author = {Selmer, Thorsten and Buckel, Wolfgang}, title = {Oxygen Exchange between Acetate and the Catalytic Glutamate Residue in Glutaconate CoA-transferase from Acidaminococcus fermentans. IMPLICATIONS FOR THE MECHANISM OF CoA-ESTER HYDROLYSIS}, series = {Journal of Biological Chemistry. 274 (1999), H. 30}, journal = {Journal of Biological Chemistry. 274 (1999), H. 30}, isbn = {1083-351X}, pages = {20772 -- 20778}, year = {1999}, language = {en} } @article{SelmerAndrei2001, author = {Selmer, Thorsten and Andrei, Paula I.}, title = {p-Hydroxyphenylacetate decarboxylase from Clostridium difficile. A novel glycyl radical enzyme catalysing the formation of p-cresol}, series = {European Journal of Biochemistry. 268 (2001), H. 5}, journal = {European Journal of Biochemistry. 268 (2001), H. 5}, isbn = {0014-2956}, pages = {1363 -- 1372}, year = {2001}, language = {en} } @article{SelmerAchebachUnden2005, author = {Selmer, Thorsten and Achebach, Stephanie and Unden, Gottfried}, title = {Properties and significance of apoFNR as a second form of air-inactivated [4Fe-4S]·FNR of Escherichia coli / Achebach, S. ; Selmer, T. ; Unden, G.}, series = {The FEBS Journal. 272 (2005), H. 16}, journal = {The FEBS Journal. 272 (2005), H. 16}, isbn = {1742-464X}, pages = {4260 -- 4269}, year = {2005}, language = {en} } @article{SelmerWillanzheimerHetzel2002, author = {Selmer, Thorsten and Willanzheimer, Angela and Hetzel, Marc}, title = {Propionate CoA-transferase from Clostridium propionicum. Cloning of the gene and identification of glutamate 324 at the active site}, series = {European Journal of Biochemistry. 269 (2002), H. 1}, journal = {European Journal of Biochemistry. 269 (2002), H. 1}, isbn = {0014-2956}, pages = {372 -- 380}, year = {2002}, language = {en} } @article{SelmerScottNaeseretal.2004, author = {Selmer, Thorsten and Scott, Richard and N{\"a}ser, Ulrike and Friedrich, Peter}, title = {Stereochemistry of hydrogen removal from the 'unactivated' C-3 position of 4-hydroxybutyryl-CoA catalysed by 4-hydroxybutyryl-CoA dehydratase / Scott, R. ; N{\"a}ser, U. ; Friedrich, P. ; Selmer, T. ; Buckel, W. ; Golding, BT.}, series = {Chemical Communications : ChemCom (2004)}, journal = {Chemical Communications : ChemCom (2004)}, isbn = {1364-548X}, pages = {1210 -- 1211}, year = {2004}, language = {en} } @article{SelmerDarleyCleggetal.2003, author = {Selmer, Thorsten and Darley, Dan J. and Clegg, William and Harrington, Ross W.}, title = {Stereocontrolled Synthesis of (2R,3S)-2-Methylisocitrate, a Central Intermediate in the Methylcitrate Cycle / Darley, Dan J. ; Selmer, Thorsten ; Clegg, William ; Harrington, Ross W. ; Buckel, Wolfgang ; Golding, Bernardt}, series = {Helvetica chimica acta. 86 (2003), H. 12}, journal = {Helvetica chimica acta. 86 (2003), H. 12}, isbn = {1522-2675}, pages = {3991 -- 3999}, year = {2003}, language = {en} } @article{MartinsBlaserFeliksetal.2011, author = {Martins, Berta M. and Blaser, Martin and Feliks, Mikolaj and Ullmann, Matthias G. and Buckel, Wolfgang and Selmer, Thorsten}, title = {Structural basis for a Kolbe-type decarboxylation catalyzed by a glycyl radical enzyme}, series = {Journal of the American Chemical Society}, journal = {Journal of the American Chemical Society}, publisher = {ACS Publications}, address = {Washington, DC}, pages = {1 -- 33}, year = {2011}, language = {en} } @article{SelmerAndreiPieriketal.2004, author = {Selmer, Thorsten and Andrei, Paula I. and Pierik, Antonio J. and Zauner, Stefan}, title = {Subunit composition of the glycyl radical enzyme p-hydroxyphenylacetate decarboxylase. A small subunit, HpdC, is essential for catalytic activity / Andrei, PI. ; Pierik, AJ. ; Zauner , S. ; Andrei-Selmer, LC. ; Selmer, T.}, series = {European Journal of Biochemistry. 271 (2004), H. 11}, journal = {European Journal of Biochemistry. 271 (2004), H. 11}, isbn = {0014-2956}, pages = {2225 -- 2230}, year = {2004}, language = {en} } @article{SelmerRecksiekDierksetal.1998, author = {Selmer, Thorsten and Recksiek, Michael and Dierks, Thomas and Schmidt, Bernhard}, title = {Sulfatases, Trapping of the Sulfated Enzyme Intermediate by Substituting the Active Site Formylglycine / Recksiek, Michael ; Selmer, Thorsten ; Dierks, Thomas ; Schmidt, Bernhard ; Figura, Kurt von}, series = {Journal of Biological Chemistry. 273 (1998), H. 11}, journal = {Journal of Biological Chemistry. 273 (1998), H. 11}, isbn = {1083-351X}, pages = {6096 -- 6103}, year = {1998}, language = {en} } @article{MuschallikMolinnusJablonskietal.2020, author = {Muschallik, Lukas and Molinnus, Denise and Jablonski, Melanie and Kipp, Carina Ronja and Bongaerts, Johannes and Pohl, Martina and Wagner, Torsten and Sch{\"o}ning, Michael Josef and Selmer, Thorsten and Siegert, Petra}, title = {Synthesis of α-hydroxy ketones and vicinal (R, R)-diols by Bacillus clausii DSM 8716ᵀ butanediol dehydrogenase}, series = {RSC Advances}, volume = {10}, journal = {RSC Advances}, publisher = {Royal Society of Chemistry (RSC)}, address = {Cambridge}, issn = {2046-2069}, doi = {10.1039/D0RA02066D}, pages = {12206 -- 12216}, year = {2020}, abstract = {α-hydroxy ketones (HK) and 1,2-diols are important building blocks for fine chemical synthesis. Here, we describe the R-selective 2,3-butanediol dehydrogenase from B. clausii DSM 8716ᵀ (BcBDH) that belongs to the metal-dependent medium chain dehydrogenases/reductases family (MDR) and catalyzes the selective asymmetric reduction of prochiral 1,2-diketones to the corresponding HK and, in some cases, the reduction of the same to the corresponding 1,2-diols. Aliphatic diketones, like 2,3-pentanedione, 2,3-hexanedione, 5-methyl-2,3-hexanedione, 3,4-hexanedione and 2,3-heptanedione are well transformed. In addition, surprisingly alkyl phenyl dicarbonyls, like 2-hydroxy-1-phenylpropan-1-one and phenylglyoxal are accepted, whereas their derivatives with two phenyl groups are not substrates. Supplementation of Mn²⁺ (1 mM) increases BcBDH's activity in biotransformations. Furthermore, the biocatalytic reduction of 5-methyl-2,3-hexanedione to mainly 5-methyl-3-hydroxy-2-hexanone with only small amounts of 5-methyl-2-hydroxy-3-hexanone within an enzyme membrane reactor is demonstrated.}, language = {en} } @article{MuschallikKippReckeretal.2020, author = {Muschallik, Lukas and Kipp, Carina Ronja and Recker, Inga and Bongaerts, Johannes and Pohl, Martina and Gelissen, Melanie and Sch{\"o}ning, Michael Josef and Selmer, Thorsten and Siegert, Petra}, title = {Synthesis of α-hydroxy ketones and vicinal diols with the Bacillus licheniformis DSM 13T butane-2, 3-diol dehydrogenase}, series = {Journal of Biotechnology}, volume = {202}, journal = {Journal of Biotechnology}, number = {Vol. 324}, publisher = {Elsevier}, address = {Amsterdam}, isbn = {2590-1559}, doi = {10.1016/j.jbiotec.2020.09.016}, pages = {61 -- 70}, year = {2020}, abstract = {The enantioselective synthesis of α-hydroxy ketones and vicinal diols is an intriguing field because of the broad applicability of these molecules. Although, butandiol dehydrogenases are known to play a key role in the production of 2,3-butandiol, their potential as biocatalysts is still not well studied. Here, we investigate the biocatalytic properties of the meso-butanediol dehydrogenase from Bacillus licheniformis DSM 13T (BlBDH). The encoding gene was cloned with an N-terminal StrepII-tag and recombinantly overexpressed in E. coli. BlBDH is highly active towards several non-physiological diketones and α-hydroxyketones with varying aliphatic chain lengths or even containing phenyl moieties. By adjusting the reaction parameters in biotransformations the formation of either the α-hydroxyketone intermediate or the diol can be controlled.}, language = {en} } @article{SelmerKahntGoubeaudetal.2000, author = {Selmer, Thorsten and Kahnt, J{\"o}rg and Goubeaud, Marcel and Shima, Seigo}, title = {The biosynthesis of methylated amino acids in the active site region of methyl-coenzyme M reductase / Selmer, Thorsten ; Kahnt, J{\"o}rg ; Goubeaud, Marcel ; Shima, Seigo ; Grabarse, Wolfgang ; Ermler, Ulrich ; Thauer, Rudolf K.}, series = {Journal of Biological Chemistry. 275 (2000), H. 6}, journal = {Journal of Biological Chemistry. 275 (2000), H. 6}, isbn = {1083-351X}, pages = {3775 -- 3760}, year = {2000}, language = {en} }