Anita Kuhn
University of Göttingen
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Archives of Microbiology | 1990
Joachim Bertram; Anita Kuhn; Peter Drre
Sixteen Tn916-induced mutants of Clostridium acetobutylicum were selected that were defective in the production of acetone and butanol. Formation of ethanol, however, was only partially affected. The strains differed with respect to the degree of solvent formation ability and could be assigned to three different groups. Type I mutants (2 strains) were completely defective in acetone and butanol production and contained one or three copies of Tn916 in the chromosome. Analysis of the mutants for enzymes responsible for solvent production revealed the presence of a formerly unknown, specific acetaldehyde dehydrogenase. The data obtained also strongly indicate that the NADP+-dependent alcohol dehydrogenase is in vivo reponsible for ethanol formation, whereas the NAD+-dependent alcohol dehydrogenase is probably involved in butanol production. No activity of this enzyme together with all other enzymes in the acetone and butanol pathway could be found in type I strains. All tetracycline-resistant mutants obtained did no longer sporulate.
Antonie Van Leeuwenhoek International Journal of General and Molecular Microbiology | 2001
Roman Grabbe; Anita Kuhn; Ruth A. Schmitz
The transcription factor Fnr (fumarate nitrate reductase regulator) globally regulates gene expression in response to oxygen deprivation in Escherichia coli. We report here the cloning and sequencing of the fnr gene from the facultative anaerobic bacterium Klebsiella pneumoniae M5al, another member of the enteric bacteria. The deduced amino acid sequence of K. pneumoniae fnr showed very high similarity (98% amino acid identity) to the Fnr protein from E. coli and contained the four essential cysteine residues which are presumed to build the oxygen-sensing [4Fe4S]+2 center. Transfer of the K. pneumoniae gene to a fnr mutant of E. coli complemented the mutation and permitted synthesis of nitrate reductase and fumarate reductase during anaerobic growth. A gene fusion between K. pneumoniae fnr and glutathione S-transferase was constructed and expressed in E. coli under anaerobic conditions in order to make the protein available in preparative amounts. The overproduced protein was purified by glutathione-Sepharose 4B affinity chromatography in the absence of oxygen, and biochemically characterized.
Fems Microbiology Reviews | 1995
Peter Dürre; Ralf-Jörg Fischer; Anita Kuhn; Karin Lorenz; Wiebke Schreiber; Benjamin Stürzenhofecker; Susanne Ullmann; Klaus Winzer; Uwe Sauer
FEBS Journal | 1973
Hans-Dieter Söling; Jochen Kleineke; Gesine Janson; Anita Kuhn; B. Willms
Applied Microbiology and Biotechnology | 1987
Peter Dürre; Anita Kuhn; Matthias Gottwald; Gerhard Gottschalk
Fems Microbiology Letters | 1998
Joseph David Santangelo; Anita Kuhn; Anke Treuner-Lange; Peter Dürre
Fems Microbiology Letters | 1986
Peter Dürre; Anita Kuhn; Gerhard Gottschalk
Applied and Environmental Microbiology | 1994
Michael Strätz; Uwe Sauer; Anita Kuhn; Peter Dürre
Fems Microbiology Letters | 1980
Friedrich Giffhorn; Anita Kuhn
FEBS Journal | 1980
Friedrich Giffhorn; Hergo Rode; Anita Kuhn; Gerhard Gottschalk