Hartmut Michel

Max Planck Institute of Biophysics


Election Year: 1996
Primary Section: 29, Biophysics and Computational Biology
Secondary Section: 21, Biochemistry
Membership Type: Foreign Associate

Research Interests

As a biochemist, I am interested in understanding the mechanism of action of those proteins that are integrated into biological membranes. The mechanism is best understood on the basis of a precisely known structure. As it is very difficult to crystallize membrane proteins, only the structures of a dozen membrane proteins are known to (nearly) atomic resolution, in contrast to the soluble proteins where several thousand structures are known. We were first successful with photosynthetic reaction centers from two different purple bacteria, followed by a light harvesting complex. The light-harvesting complex absorbs light and transfers its energy to the reaction center, which catalyzes the light-driven transfer of electrons across the photosynthetic membrane. A more recent success was our crystallization and structure determination of the terminal enzyme of the respiratory chain, cytochrome c oxidase. This enzyme combines electrons from cytochrome c with molecular oxygen and protons to form water. The energy is used to "pump" protons across mitochondrial or bacterial membranes. The challenge now is to determine how this process occurs. The absence of structural knowledge with membrane integrated receptors, channel proteins, and translocators is also based on the lack of sufficient material. We therefore work on methods to produce these proteins using recombinant DNA technology.

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