Hartmut Michel

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Hartmut Michel
Michel, Hartmut (1948).jpg
Hartmut Michel in 2013
Born (1948-07-18) 18 July 1948 (age 73)
Ludwigsburg
NationalityGerman
Alma materUniversity of Tübingen
Known forCrystallisation of membrane proteins
Spouse(s)Elena Olkhova
Awards
Scientific career
FieldsBiochemistry
InstitutionsMax Planck Institute for Biophysics
Websitewww.biophys.mpg.de/en/michel.html

Hartmut Michel (born 18 July 1948) is a German biochemist, who received the 1988 Nobel Prize in Chemistry for determination of the first crystal structure of an integral membrane protein, a membrane-bound complex of proteins and co-factors that is essential to photosynthesis.[2][3][4][5]

Education and early life[]

He was born on 18 July 1948 in Ludwigsburg. After compulsory military service, he studied biochemistry at the University of Tübingen, working for his final year at Dieter Oesterhelt's laboratory on ATPase activity of halobacteria.

Career and research[]

Hartmut later[when?] worked on the crystallisation of membrane proteins - essential for their structure elucidation by X-ray crystallography. He received the Nobel Prize jointly with Johann Deisenhofer and Robert Huber in 1988. Together with Michel and Huber, Deisenhofer determined the three-dimensional structure of a protein complex found in certain photosynthetic bacteria. This membrane protein complex, called a photosynthetic reaction center, was known to play a crucial role in initiating a simple type of photosynthesis. Between 1982 and 1985, the three scientists used X-ray crystallography to determine the exact arrangement of the more than 10,000 atoms that make up the protein complex. Their research increased the general understanding of the mechanisms of photosynthesis, revealed similarities between the photosynthetic processes of plants and bacteria and established a methodology for crystallising membrane proteins.[6]

Since 1987 he has been director of the Molecular Membrane Biology department at the Max Planck Institute for Biophysics in Frankfurt am Main, Germany, and professor of biochemistry at the Goethe University Frankfurt.

Awards and honours[]

In 1986, he received the Gottfried Wilhelm Leibniz Prize of the Deutsche Forschungsgemeinschaft, which is the highest honour awarded in German research. In 1988, he received the Nobel Prize in Chemistry. He received the Bijvoet Medal at the Bijvoet Center for Biomolecular Research of Utrecht University in 1989.[7] In 1995 he became a member of the German Academy of Sciences Leopoldina.[8] He also became a foreign member of the Royal Netherlands Academy of Arts and Sciences in 1995.[9] He was elected a Foreign Member of the Royal Society (ForMemRS) in 2005.[1]

References[]

  1. ^ Jump up to: a b "Professor Hartmut Michel ForMemRS". London: Royal Society. Archived from the original on 26 October 2015.
  2. ^ "Autobiographical information on Hartmut at www.nobel.org".
  3. ^ "P3 Hartmut Michel". www.sfb807.de.
  4. ^ Iwata, S.; Ostermeier, C.; Ludwig, B.; Michel, H. (1995). "Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans". Nature. 376 (6542): 660–9. Bibcode:1995Natur.376..660I. doi:10.1038/376660a0. PMID 7651515. S2CID 4345523.
  5. ^ Deisenhofer, J.; Epp, O.; Miki, K.; Huber, R.; Michel, H. (1984). "X-ray structure analysis of a membrane protein complex". Journal of Molecular Biology. 180 (2): 385–98. doi:10.1016/S0022-2836(84)80011-X. PMID 6392571.
  6. ^ Deisenhofer, J.; Epp, O.; Miki, K.; Huber, R.; Michel, H. (1985). "Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3Å resolution". Nature. 318 (6047): 618–24. Bibcode:1985Natur.318..618D. doi:10.1038/318618a0. PMID 22439175. S2CID 1551692.
  7. ^ "Bijvoet Medal". Bijvoet Center for Biomolecular Research. Archived from the original on 12 September 2017. Retrieved 12 September 2017.
  8. ^ "Hartmut Michel". German Academy of Sciences Leopoldina. Retrieved 1 June 2021.
  9. ^ "H. Michel". Royal Netherlands Academy of Arts and Sciences. Archived from the original on 13 February 2016. Retrieved 13 February 2016.

External links[]

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