Rudolf K. Thauer

thauer rudolf

 

Biochemistry, physiology and ecology of anaerobic bacteria and archaea with a focus on the enzymes and coenzymes involved in the energy metabolism of Clostridia, of sulfate-reducing bacteria and archaea, and of methanogenic- and methanotrophic archaea. Recent papers were on the structure and function of [Fe]-hydrogenase (Hmd) and methyl-coenzyme M reductase and on flavin-based electron bifurcation as novel mechanism of energy conservation. It was reported together with Seigo Shima that [Fe]-hydrogenase harbors a novel iron-guanylylpyridinol cofactor whose structure was elucidated. Methyl-coenzyme M reductase was shown for the first time to also catalyze the anaerobic oxidation of methane. And together with Wofgang Buckel it was found that flavin-based electron bifurcation allows the coupling of endergonic- to exergonic reactions by cytoplasmic enzymes. This coupling mechanism is key to the understanding of the energy metabolism of methanogens, of acetogens, of Clostridia and of many other anaerobes.

 

Please visit: http://www.mpi-marburg.mpg.de/thauer/

 

 


 

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