MICHEL Harmut( Chemist, Nobel Prize in Chemistry, 1988)
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Biography MICHEL Harmut
Michel, HARMUT (Michel, Hartmut) (p. 1948) (FRG). Nobel Prize in Chemistry, 1988 (with I. Dayzenhoferom and R. Huber).
Born in g.Lyudvigsberge in Wц+rttemberg (southwest Germany) July 18, 1948. The eldest son of Charles and Frieda Michel, carpenter and a housewife.
In school, favorite subjects were history, biology, chemistry and physics. Particular pleasure he gave the study of physics. Basic understanding of the subject were laid in the school, not university.
Interest in molecular biology led him in 1969 in Tubingen University - the only place where it was possible to study biochemistry in the first year. In addition, it was possible to work during the year (1972-1973) in biochemical laboratories of the University of Munich and the Max Planck Institute of Biochemistry.
The experimental part of degree work completed under the guidance of Michael Oysterhelda Dieter (Dieter Oesterhelt) at the Friedrich Miescher Laboratory of the Max Planck Society in Tц+bingen. Oysterheld bacteriorhodopsin studied halophilic and thought that (in hemoosmoticheskoy theory) it acts as a proton pump svetozavisimy P. Mitchell (Nobel Laureate, 1978) and ATP-aznuyu activity of these halophilic.
In 1975 Oysterheld moved to Wц+rzburg, and Michael followed him. In his dissertation, he established a correspondence between the intracellular levels of ADP and ATP and the electrochemical gradient of hydrogen ions on the cell membrane of halophilic. After receiving his doctorate in June 1977, he tried to link low-fat bacteriorhodopsin with bacterial vesicles and found that the result is a solid glass-formation. First there was the possibility crystallize membrane proteins such as bacteriorhodopsin, that seemed impossible. Four weeks after the first observation of two-dimensional crystal of membrane bacteriorhodopsin was obtained. The first three-dimensional crystals of bacteriorhodopsin were prepared by him in April 1979, however, these crystals were found to cause too small and messy for the structural analysis of the diffraction of X-rays.
Michael again moved for Oysterheldom, this time at the Max Planck Institute for Biochemistry in Martinsried, where he headed the department and became director. The decisive factor was the move to joint work with R. Huber and I. Dayzenhoferom from the Department of X-ray crystallographic analysis of protein structures.
In the absence of final successful result in the experiments with bacteriorhodopsin. Michael attempted crystallization of some other membrane proteins, mainly photosynthetic. In late July 1981, he received the first crystals of photosynthetic reaction center from purple bacterium Rhodopseudomonas viridis.
In April-May 1982, Michael proposed formal cooperation P. Huber, head of the laboratory X-ray crystallographic analysis of protein structures in the Max Planck Institute of Biochemistry in Martinsried near Munich. In partners to Michael that highlighted I. Dayzenhofera.
In August 1982 Dayzenhofer begin processing X-ray data. Michael continued his experimental work, sometimes it helped Huber, who explained how to look diffraction pattern of the expected derivative.
However, for the interpretation of X-ray analysis of the data needed was a complete biochemical characterization of the object, and identification of amino acid sequences. After a preliminary tagging of peptide chains, performed Dayzenhoferom, this part of the study, which was conducted, Michael, was the most difficult portion of. Nevertheless, and it was successfully completed.
It took another two years before it was re-established the full structure of the reaction center and another two years before the accuracy of reconstruction was so close to a 2,3 A.
In 1988, along with Michael R. Huber and I. Dayzenhoferom received the Nobel Prize 'for determining the three-dimensional structure of the photosynthetic reaction center'.
Since October 1987, Michael became head of the Max Planck Institute for Biophysics in Frankfurt. In 1988, Michael crystallized and determined the structure of the terminal dyhatelnogo enzyme.