TY - CHAP A1 - Walenta, Robert A1 - Schellekens, Twan A1 - Ferrein, Alexander A1 - Schiffer, Stefan T1 - A decentralised system approach for controlling AGVs with ROS T2 - AFRICON, Proceedings Y1 - 2017 SN - 978-1-5386-2775-4 U6 - http://dx.doi.org/10.1109/AFRCON.2017.8095693 SN - 2153-0033 N1 - AFRICON <2017, 18-20 Sept., Cape Town, South Africa> SP - 1436 EP - 1441 PB - IEEE ER - TY - CHAP A1 - Funke, Harald A1 - Beckmann, Nils A1 - Abanteriba, Sylvester T1 - A comparison of complex chemistry mechanisms for hydrogen methane blends based on the Sandia / Sydney Bluff-Body Flame HM1 T2 - Proceedings of the Eleventh Asia‐Pacific Conference on Combustion (ASPACC 2017), New South Wales, Australia, 10-14 December 2017 Y1 - 2017 SN - 978-1-5108-5646-2 SP - 262 EP - 265 ER - TY - JOUR A1 - Wilke, Thomas T1 - [Rezension zu:] Deutsch, Kristina: Jean Marot. Un graveur d'architecture à l'époque de Louis XIV. (= Ars et Scientia; 12), Berlin; Boston 2015. JF - ArtHist.net Y1 - 2017 ER - TY - JOUR A1 - Muschallik, Lukas A1 - Molinnus, Denise A1 - Bongaerts, Johannes A1 - Pohl, Martina A1 - Wagner, Torsten A1 - Schöning, Michael Josef A1 - Siegert, Petra A1 - Selmer, Thorsten T1 - (R,R)-Butane-2,3-diol Dehydrogenase from Bacillus clausii DSM 8716T: Cloning and Expression of the bdhA-Gene, and Initial Characterization of Enzyme JF - Journal of Biotechnology N2 - The gene encoding a putative (R,R)-butane-2,3-diol dehydrogenase (bdhA) from Bacillus clausii DSM 8716T was isolated, sequenced and expressed in Escherichia coli. The amino acid sequence of the encoded protein is only distantly related to previously studied enzymes (identity 33–43%) and exhibited some uncharted peculiarities. An N-terminally StrepII-tagged enzyme variant was purified and initially characterized. The isolated enzyme catalyzed the (R)-specific oxidation of (R,R)- and meso-butane-2,3-diol to (R)- and (S)-acetoin with specific activities of 12 U/mg and 23 U/mg, respectively. Likewise, racemic acetoin was reduced with a specific activity of up to 115 U/mg yielding a mixture of (R,R)- and meso-butane-2,3-diol, while the enzyme reduced butane-2,3-dione (Vmax 74 U/mg) solely to (R,R)-butane-2,3-diol via (R)-acetoin. For these reactions only activity with the co-substrates NADH/NAD+ was observed. The enzyme accepted a selection of vicinal diketones, α-hydroxy ketones and vicinal diols as alternative substrates. Although the physiological function of the enzyme in B. clausii remains elusive, the data presented herein clearly demonstrates that the encoded enzyme is a genuine (R,R)-butane-2,3-diol dehydrogenase with potential for applications in biocatalysis and sensor development. Y1 - 2017 U6 - http://dx.doi.org/10.1016/j.jbiotec.2017.07.020 SN - 0168-1656 VL - 258 SP - 41 EP - 50 PB - Elsevier CY - Amsterdam ER -