Hartmut Michel | Biography

Hartmut Michel was born July 18, 1948, in Ludwigsburg, Germany, to Karl and Freda Kachler Michel. Michel graduated in 1967 from the Friedrich Schiller Gymnasium, with a strong interest in molecular biology and biochemistry, but before pursuing his education, served for two years in the military. In 1969, Michel enrolled in the University of Tubingen. During 1972, he did laboratory work at the University of Munich and at the Max Planck Institute for Biochemistry at Martinsred, and by the end of that year he had decided to pursue a career in academic research. Michel passed his exams in 1974, and began work in the Friedrich Miescher Laboratory of the Max Planck Society in Tubingen under Dieter Oesterhelt, a biochemist. Oesterhelt moved to the University of Wurzburg in 1975, and Michel went with him. It was here he completed work for his Ph.D. in 1977.

A good portion of Michel's work under Oesterhelt was devoted to the study of photosynthesis, considered by scientists as the most important chemical reaction in the biosphere. At its most basic level, photosynthesis is the conversion of water and carbon dioxide with the use of sunlight into oxygen and nutrients, but the process is actually extremely complicated and not well understood. At the time Michel began his work, it was surmised that an area of protein, known as the photosynthetic reaction center, was a major actor in the process of photosynthesis; scientists believed that the electrons somehow picked up the charge that drove the reaction here, but little else was known about it.

Scientists usually study proteins, as they study many substances, by crystallizing them. The crystallized form of a substance is a good subject because crystals are characterized by a very organized internal atomic structure--they are predictable solids. X-ray crystallography is a tool commonly used in analysis of crystals; Michel's difficulty was in finding a method to create a crystal out of the protein. It was considered almost impossible to crystallize membrane proteins, the type present in the photosynthetic reaction center. Water is generally used in crystallization, but membrane proteins interact with water as part of their function, so they are not water soluble. Michel decided that this did not mean membrane proteins could not be crystallized, but that they must be crystallized with a different solution. He originally worked on this problem with bacteriorhodopsin, one of the halobacteria, which means salt-loving. By using different detergents instead of water, he was able to form a two-dimensional crystal and a very small three-dimensional crystal, neither suitable for study with X-ray crystallography.

At this point in his research, Michel had planned to pursue a postdoctoral position. His limited success, however, excited him enough to move once again with Oesterhelt, this time to the Max Planck Institute for Biochemistry in Martinsred in 1979. Once settled, Michel decided to try a different membrane protein, choosing that of rhodopseudomonas viridis, a purple bacterium containing the simplest known photosynthetic reaction center. Success came two years later; in 1981 he formed a crystal that could be studied.

With a crystal well-formed enough to study, Michel turned to Robert Huber, a department head at the Max Planck Institute, to help find a suitable expert in X-ray crystallography to run the tests. Huber directed Michel to Johann Deisenhofer, and a four-year collaboration was begun. By the end of this period, they had identified and placed more than 10,000 atoms in the membrane protein. This work led to the award of the 1988 Nobel Prize in chemistry to Michel, Huber, and Deisenhofer. In receiving this award, the scientists were credited for work which had implications far beyond photosynthesis, including the understanding of respiration, nerve impulses, hormone action, and the process of nutrient introduction to the cells. The understanding of photosynthesis alone, however, is an important advance in scientific knowledge, and would have implications for many aspects of technology.

Before the award of the Nobel Prize, Michel won two other awards jointly with Deisenhofer--the Biophysics Prize of the American Physical Society in 1986, and the Otto-Bayer Prize in 1988. Michel was also the recipient of the 1986 Otto Klung Prize for Chemistry and the Leibniz Prize of the German Research Association in 1986. Michel is a member of the European Molecular Biology Organization, the Max Planck Society, the Society for Biological Chemistry, the German Chemists' Society, and the Society for Physical Biology. In 1987, he was named department head and director at the Max Planck Institute for Biophysics in Frankfurt/Main. His work continues there in the areas of photosynthesis and crystallization. Michel was editor of Crystallization of Membrane Proteins in 1989.

Michel has been married to Ilona Leger-Michel since 1979. They have a son and a daughter together, and a daughter from his wife's previous marriage. In his spare time, Michel enjoys reading history, traveling, and growing orchids.