Personal information

1939 born in Berlin 

1964 Diploma in Chemistry, University of Freiburg

1968 Dr. rer.nat. University of Freiburg (Supervisor Kurt Wallenfels)

1969-1970 Postdoctoral Fellow with Lester Reed, University of Texas at Austin

1971 Research Assistant University of Konstanz

1973 Research at the Institut Pasteur, Paris, with J.-P. Changeux

1974 Habilitation, Biochemistry

1978 Associate Professor University of Konstanz

1979 Associate Professor Freie Universität Berlin 

1989 Several offers of Chairs at German Universities 

1990 Chair of Biochemistry, Freie Universität Berlin 

1997-1999 Dean of the Chemistry Department

1997 Member of the Berlin-Brandenburg Academy of Sciences and Humanities,

2002-2008 Sekretar (Speaker) of the Bioscience/Medical Section, Member of the Board of the Academy

1994 Treasurer,

2001-2005 President of the European Society of Neurochemistry (ESN) 

Member of the Council of the ISN (1999-2003), Editorial Board of FEBS Journal (Reviews Editor) and various Scientific journals.

Selected publications

  1. Krabben L., vanRossum B.J., Jehle S., Bocharov E., Lyukmanova E.N., Schulga A.A., Arseniev A., Hucho F., Oschkinat H. (2009). Loop 3 of short neurotoxin II is an additional interaction site with membrane-bound nicotinic acetylcholine receptor as detected by solid-state NMR spectroscopy. J. Mol. Biol. 390 (4), 662–71 [+]

    The contact area of neurotoxin II from Naja naja oxiana when interacting with the membrane-bound nicotinic acetylcholine receptor from Torpedo californica was determined by solid-state, magic-angle spinning NMR spectroscopy. For this purpose, the carbon signals for more than 90% of the residues of the bound neurotoxin were assigned. Differences between the solution and solid-state chemical shifts of the free and bound form of the toxin are confined to distinct surface regions. Loop II of the short toxin was identified as the main interaction site. In addition, loop III of neurotoxin II shows several strong responses defining an additional interaction site. A comparison with the structures of alpha-cobratoxin bound to the acetylcholine-binding protein from snail species Lymnaea stagnalis and Aplysia californica, and of alpha-bungarotoxin bound to an extracellular domain of an alpha-subunit of the receptor reveals different contact areas for long and short alpha-neurotoxins.

  2. Machold J., Utkin Y., Kirsch D., Kaufmann R., Tsetlin V., Hucho F. (1995). Photolabeling reveals the proximity of the alpha-neurotoxin binding site to the M2 helix of the ion channel in the nicotinic acetylcholine receptor. Proc. Natl. Acad. Sci. U.S.A. 92 (16), 7282–6 [+]

    For the first time the amino acid residue labelled by photoactivatable neurotoxin derivative was localized in amino acid sequence of nicotinic acetylcholine receptor. Basing on these data the position of neurotoxin molecule on the receptor was established. The toxin molecule is located much closer to membrane surface than it was accepted earlier.

  3. Kreienkamp H.J., Utkin Y.N., Weise C., Machold J., Tsetlin V.I., Hucho F. (1992). Investigation of ligand-binding sites of the acetylcholine receptor using photoactivatable derivatives of neurotoxin II from Naja naja oxiana. Biochemistry 31 (35), 8239–44 [+]

    In this work the subunits of muscle-type receptor participating in formation of binding sites for agonist/competitive antagonists were established by use of photoactivatable neurotoxin derivatives.