Hartmut Michel
Max Planck Institute of Biophysics
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Primary Section: 29, Biophysics and Computational Biology Secondary Section: 21, Biochemistry Membership Type:
International Member
(elected 1996)
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Biosketch
As a trained biochemist I try to understand biological reactions in atomic details which requires knowledge of atomic structures. We have a focus on membrane proteins. Having invented methods for membrane protein crystallization I received the Nobel Prize in Chemistry already at age 40 "for the determination of the three-dimensional structure of a photosynthetic reaction center". My current position as a director at a Max Planck Institute, that of Biophysics in Frankfurt am Main, Germany, allows me to tackle many interesting projects. My research interest shifted from photosynthesis to cellular respiration and active transport across membranes. With "resolution revolution" in electron microscopy the tedious and risky crystallization of membrane proteins is no longer required and we use preferentially electron cryomicroscopy instead of X-ray crystallography. We hope to contribute to fight diseases like tuberculosis and cancer with our current research.
Research Interests
With our current research we try to understand the complexes of the respiratory chain, in particular the terminal oxidases that reduce molecular oxygen to water and provide most of the energy of living systems. We have determined the structures of members of all families of terminal oxidases. Now the challenge is: How do they work? In addition we work on secondary active transporters like the sodium ion/proton exchanger NhaA, the members of the drug resistance causing transporter of the MATE family, and various amino acid transporters from humans. Protein production is a bottleneck. We have a focus on method development because the development of novel methods determines the speed of scientific progress.
