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Peter Dimroth
Peter Dimroth (born 13 November 1940 in Göttingen, Germany) is a German chemist and biochemist. He is professor emeritus at the ETH Zürich, Switzerland.

1 Life
Peter Dimroth studied chemistry in Marburg, Freiburg and Munich from 1960 to 1965. In 1969 he earned his doctorate at the Max-Planck-Institute for Cell Chemistry in Munich, under guidance of Feodor Lynen. From 1969-1971 Peter Dimroth was a postdoctoral fellow at the New York University, New York City and the Johns Hopkins University, Baltimore. After returning to Germany in 1971, Peter Dimroth was a research assistant and group leader at the University of Regensburg for 8 years. From 1980-1990, he was appointed as professor of physiological chemistry at the Technical University of Munich. In 1990, Peter Dimroth became professor of microbiology at the ETH Zürich in Switzerland, where he worked until his retirement in 2005.

2 Work
Peter Dimroth’s research focused on bacterial metabolism and bioenergetics. He made the pivotal discovery that sodium ions can replace protons for energy conservation and chemiosmotic ATP synthesis discovered by Peter D. Mitchell. Peter Dimroth pioneered the functional and structural characterization of membrane-bound enzyme complexes essential for the generation of a electrochemical sodium gradient and its utilization for ATP synthesis. He discovered and mechanistically analyzed several classes of sodium-dependent enzyme complexes, such as ion transport decarboxylases, FoF1 ATP synthases and NADH:ubiquinone oxidoreductase oxidoreductases. Peter Dimroth studies led him to coin the term “decarboxylation phosphorylation”, which is now recognized as the third mode of ATP synthesis besides oxidative phosphorylation and substrate level phosphorylation. His major contributions are of fundamental importance for the fields of microbiology and biochemistry. In addition to his scientific achievements, Peter Dimroth was a dedicated teacher, training almost 40 Ph.D. students and postdocs, many of whom moved on to become academic researches themselves.

3 Awards
1977 Karl-Winnacker-Prize

4 References

 * 1) Hilpert, W., Dimroth, P. (1982) Conversion of the chemical energy of methylmalonyl CoA decarboxylation into a Na+ gradient. Nature (London) 296, 584-585.
 * 2) Hilpert, W., Schink, B., Dimroth, P. (1984) Life by a new decarboxylation-dependent energy conservation mechanism with Na+ as coupling ion. EMBO J. 3, 1665-1670
 * 3) Laubinger, W., Dimroth, P. (1987) Characterization of the Na+-stimulated ATPase of Propionigenium modestum as an enzyme of the F1Fo type. Eur. J. Biochem. 168, 475-480.
 * 4) Dimroth, P. (1989) Mechanisms of Na+ transport in bacteria. Phil. Trans. R. Soc. Lond. B 326, 465-477.
 * 5) Pfenninger-Li, X.D., Dimroth, P. (1995) The Na+-translocating NADH:ubiquinone oxidoreductase from the marine bacterium Vibrio alginolyticus contains FAD but not FMN.FEBS Lett. 369, 173-176.
 * 6) Dimroth, P. (1997) Primary sodium ion translocating enzymes. Biochim. Biophys. Acta 1318, 11-51
 * 7) Dimroth, P., Jockel, P., Schmid, M. (2001) Coupling mechanism of the oxaloacetate decarboxylase Na+ pump.Biochim. Biophys. Acta 1505, 1-14.
 * 8) Von Ballmoos, C., Appoldt, Y., Brunner, J., Granier, T., Vasella, A., Dimroth, P. (2002) Membrane topography of the coupling ion binding site in Na+-translocating F1F0 ATP synthase. J. Biol. Chem. 277, 3504-3510.
 * 9) Meier T, Polzer P, Diederichs K, Welte W, Dimroth P. (2005) Structure of the rotor ring of F-Type Na+-ATPase from Ilyobacter tartaricus. Science 308, 659-62

5 External links

 * http://www.mpg.de/en
 * http://www.nobelprize.org/nobel_prizes/medicine/laureates/1964/
 * http://www.nyu.edu/
 * https://www.jhu.edu/
 * http://www.nobelprize.org/nobel_prizes/chemistry/laureates/1978/mitchell-bio.html