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Max Perutz and the Structure of Hemoglobin

      Hemoglobin is the critical oxygen-carrying protein in mammalian blood. Hemoglobin’s unique physical structure – four globular proteins that surround an iron-containing heme group – facilitates its ability to efficiently transport both oxygen and carbon dioxide. In 1962, Cambridge (UK)-based molecular biologist Max Perutz shared the Nobel Prize in Physiology or Medicine with another structural biologist from Cambridge, John Kendrew, for the 1959 discovery of the structure of hemoglobin and a related oxygen-carrying protein found in muscles, myoglobin.
      Perutz was born in Vienna in 1914 to Adele Goldschmidt and Hugo Perutz, non-observant Jews who baptized their son in the Catholic Church. Hugo Perutz was a well-to-do textile manufacturer. As therapy for tuberculosis, Perutz's mother encouraged him to ski and climb mountains. Despite his parents’ wishes for him to become a lawyer, Max Perutz developed an interest in chemistry and chose to study this subject at the University of Vienna, graduating in 1936. Following graduation, he worked at the Cavendish Laboratory in Cambridge under the direction of John Desmond “Sage” Bernal, who focused on X-ray crystallography of proteins, a topic which then became Perutz’ primary research focus for the rest of his career.
      William Lawrence Bragg, discoverer of the Bragg law of X-ray diffraction and Nobel Prize laureate in Physics in 1915 (together with his father, William Henry Bragg), served as Perutz’s doctoral thesis advisor. Perutz persisted with his crystallography work despite discouragement from some colleagues, who pointed out that the crystal structure of simple sugars had not yet been solved, so understanding a complex molecule like hemoglobin seemed an impossible task. While in Cambridge, Perutz was supported initially by his father’s money. He chose to join Peterhouse college because it had “the best food.”
      In 1938, Germany annexed Austria and the Perutz family fled to Switzerland, leaving all their money behind and therefore no longer able to support their son in Cambridge. That summer Max was invited to join a research team studying glaciers in the Swiss Alps, because of his interest in crystals and childhood mountaineering experience. After the summer research ended, a grant from the Rockefeller Foundation to study hemoglobin gave him enough money to support his own work and pay for his parents’ passage out of Continental Europe. However, a few months later he was exiled to Newfoundland as an “enemy alien,” along with many other residents of German or Austrian descent in the British Isles. With political intervention from his friends, he was returned to England a few months later and assigned to war projects, including an unrealized plan to build a floating mid-Atlantic aircraft landing platform from ice. In 1940, his PhD thesis was accepted.
      Perutz married a German refugee, Gisele Peiser, in 1942, and they had two children. In 1947, Perutz and Bragg convinced the Medical Research Council (MRC) to support a molecular biology research unit in Cambridge. This unit attracted a number of excellent scientists, including Francis Crick and James Watson; Rosalind Franklin’s x-ray crystallography work led to Crick and Watsons’ discovery of the double helical structure of DNA. In 1962 a new MRC Laboratory of Molecular Biology was established in Cambridge, with Perutz as its head. By 1970 Perutz had solved the crystal structure of hemoglobin in both oxygenated and deoxygenated states.
      In later years, Perutz studied the protein that causes Huntington disease and also wrote frequently for a general audience, winning awards such as the 1997 Lewis Thomas Prize for Science Writing for his lucid presentations of scientific and philosophical issues. He was made a Fellow of The Royal Society in 1954, Commander of the British Empire in 1962, and received the Order of Merit in 1988. He died in 2002, and was honored philatelically by the United Kingdom in 2014 as part of the Royal Mail’s “Remarkable Lives” series (Scott #pending).