Robert Huber was born on February 20, 1937 in Munich, Germany to Sebastian and Helen Kebinger Huber. In 1947 Huber entered the Humanistisches Karls-Gymnasium in Munich, a school with an emphasis on humanistic studies. It was here he developed an interest in chemistry. In 1956 he graduated from the gymnasium and entered the Technische Hochschule of Munich--later renamed the Technical University--to study chemistry. He graduated in 1960, and married Christa Essig that same year. They would have four children together.
As a graduate student, Huber worked with a number of prominent chemists, including Walter Hieber in the field of inorganic chemistry, Ernst Fischer who studied organometallic chemistry, and F. Weygand in organic chemistry. But it was crystallography that won Huber's interest. Though his thesis work for his 1963 doctorate was done on the crystal structure of a diazo compound, it was crystallographic studies on the insect metamorphosis hormone ecdysone that set him on the path of x-ray crystallography. Working with Hoppe at both the Technical University and at the Physiological-Chemical Institute of the University of Munich, Huber was able to determine the molecular weight and steroid nature of ecdysone. He employed x-ray diffraction techniques (where an x-ray beam is shot at a crystallized substance) to determine the atomic structure of ecdysone by analyzing how the beam was dispersed by the crystal. Huber was so impressed by the results he attained that he decided to concentrate on crystallographic research.
After determining the structure of several organic compounds and developing some improvements in existing x-ray crystallography methods, in 1967 Huber and H. Formanek set out to elucidate the structure of erythrocruorin, an insect protein. Their results showed a marked similarity between erythrocruorin and mammalian proteins. Their work also suggested for the first time that there might be a universal globin fold--the globin fold being the manner in which the chain of amino acids constituting the protein folds upon itself, endowing the protein with a shape specific to its function. In 1968, Huber became a lecturer at the Technical University, and three years later he accepted a position as a director at the prestigious Max Planck Institute for Biochemistry at Martinsried near Munich. He maintained his affiliation with the Technical University as well, becoming a full professor there in 1976.
Throughout the 1970s, Huber and his co-workers refined and perfected the techniques of x-ray crystallography, elucidating the structures of various proteins in collaboration with both foreign and domestic laboratories. His work in enzyme inhibitors and immunoglobulins has been of particular interest to researchers developing technologies for drug and protein design.
In 1982 a fellow researcher at Martinsried named Hartmut Michel came to Huber with a monumental task: to elucidate the atomic structure of the protein complex that powers photosynthesis in the purple bacteria, Rhodopseudomonas viridis. Michel had managed to isolate and crystallize a protein complex known as a membrane-bound protein, which is situated on the outer membrane of the bacterium. These proteins, made up of a tangle of four protein subunits and molecules of chlorophyll, help transport energy across the walls of cells. Yet they had been extremely difficult to isolate, because of their intermediary position on the membrane wall. Many believed these proteins were impossible to isolate, but by 1982 Michel had grown crystals of this protein complex, which functions as a photosynthesis reaction center. The reaction center is the place where electrons--released by a photon-excited chlorophyll molecule--create an electrical charge difference that produces the energy to power the synthesis of chemical compounds such as sugar, carbohydrates, and other nutrients.
Huber agreed to take on the task of developing a structural analysis of the proteins Michel had crystallized. Working with German biochemist Johann Deisenhofer at Martinsried and several other biochemists, his team used their improved x-ray crystallographic techniques to determine the exact atomic structure of the reaction center. By 1985 they had mapped over 10,000 separate atoms, and their structural analysis confirmed predictions as to the path that electrons follow in the reaction center. Though there are significant differences in the process of photosynthesis in green plants and in bacteria, the three-dimensional atomic model that Deisenhofer and Huber developed has proved to be of immense importance in further photosynthesis research in general. It has also been vital in research into the part that membrane-bound proteins may play in diseases such as cancer and diabetes. The work of the three main researchers in this project--Huber, Michel, and Deisenhofer--was recognized by a joint award of the Nobel Prize for chemistry in 1988.
Huber has also been instrumental in developing computer models, such as FILME, PROTEIN, FRODO, and MADNESS to help in determining atomic structures through x-ray crystallography. Besides the Nobel Prize, Huber's work has been recognized by the E. K. Frey Medal from the German Society for Surgery in 1972, and the Otto Warburg Medal from the German Society for Biological Chemistry in 1977. He has received the Emil von Behring Medal from the University of Marburg in 1982, and the Keilin Medal from the London Biochemical Society and the Richard Kuhn Medal from the Society of German Chemists, both in 1987, as well as the Sir Hans Krebs Medal in 1992. He has also received numerous honorary doctorates and memberships in foreign chemical and biochemical societies.
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