Origin of Life

Jan R. Andreesen

Last Event

10th June 2016, 16:15
Astrophysical Sources of Energy for Life



Jan Remmer Andreesen, born 1941, received a "Dr. rer. nat” degree from the University of Göttingen, for work on isolation and characterization of new anaerobic CO2-reducing acetogenic bacteria (supervisor Gerhard Gottschalk) after studying in Hamburg, Tübingen and Göttingen. He continued biochemical work on the action of trace elements such as selenium (Se) and tungsten (W) on CO2-reducing formate dehydrogenases (FDH) at the University of Georgia in Athens, USA, working for two years with Lars G. Ljungdahl. In 1972 he returned to Göttingen and established the role of Se and W for FDH-activity and for Se for some xanthine dehydrogenases of anaerobes. From 1993 to 2007 he was head of the microbiology department of The University of Halle/S. He expanded his interests to general mechanisms for degradation of heterocyclic compounds and of the amino acids glycine and proline serving as electron acceptors in Stickland reactions and to selective uptake of anions.


Selected papers


Fonknechten N, Chaussonnerie S, Tricot S, Lajus A, Andreesen JR, Perchat N, Pelletier E, Gouyvenoux M, Barbe V, Salanoubat M, Le Paslier D, Weissenbach J, Cohen GN, Kreimeyer A (2010) Clostridium sticklandii, a specialist in amino acid degradation: revisiting its metabolism through its genome sequence. BMC Genomics 11, 555.


Andreesen JR, Makdessi K (2008) Tungsten, the surprisingly positively acting heavy metal element for prokaryotes. Ann N Y Acad Sci 1125, 215-229.


Andreesen JR (2005) Degradation of heterocyclic compounds, in: Handbook on Clostridia, P. Dürre ed., CRC Press, Boca Raton, FL, pp.221-238.


Andreesen JR (2004) Glycine reductase mechanism. Curr Opin Chem Biol 8, 454-461.


Graentzdoerffer A, Rauh D, Pich A, Andreesen JR (2003) Molecular and biochemical characterization of two tungsten- and selenium-containing formate dehydrogenases from Eubacterium acidaminophilum that are associated with components of an iron-only hydrogenase. Arch Microbiol 179, 116-130.

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