Max F. Perutz

Max F. Perutz (1914-2002), Austrian-born British biochemist and Nobel Prize winner. Perutz's work with protein structures, particularly that of hemoglobin (the pigment in blood cells that carries oxygen to the body's tissues), ultimately produced great strides in the advances of molecular biology. Perutz won the 1962 Nobel Prize in chemistry, which he shared with British chemist Sir John Kendrew.

Perutz was born in Vienna, Austria. In 1932 he entered Vienna University and graduated with a degree in organic chemistry in 1936. The same year he started doctoral studies at the University of Cambridge in England and received his doctorate in chemistry in 1940. While studying the biological use of X-ray crystallography in 1937 at the University of Cambridge in England, he became convinced of the importance of understanding hemoglobin's structure in order to solve other mysteries of physiology. Working with horse-hemoglobin crystals, Perutz studied hemoglobin's large crystal structure, which is thousands of times more complex than those of the simple metal, mineral, and salt crystals that had previously been the focus of crystallography.

During World War II (1939-1945) Perutz was arrested as an “enemy alien” by the British government and spent two years (1941-1943) in prison camps. Undaunted, he organized camp “universities” among the many scientists and intellectuals who were also imprisoned; the captive academics taught courses in their specialties to one another. In 1943 he was released from his internment to work on a war-related project and by 1945 Perutz and other colleagues were permitted to resume their work in England. Perutz met Kendrew when they were working in the Cavendish Laboratory at Cambridge in 1946. They worked together along with Francis Crick, James Watson, and Frederick Sanger as they developed the technique of X-ray crystallography. Later they worked separately as Kendrew determined the structure of the myoglobin molecule and Perutz studied the hemoglobin molecule. In 1947 he and Kendrew founded the Medical Research Council Unit for Molecular Biology at Cambridge, where Perutz continued to refine X-ray crystallography technology.

Perutz was able to construct a model of hemoglobin and later helped prove that hemoglobin's molecular structure changes when it reacts with oxygen. Perutz's discovery resulted in a better understanding of how hemoglobin absorbs and releases oxygen. His work with sickle-cell anemia led to the discovery that it is a change in the hemoglobin molecule's shape that initiates the red cells' distortion into a sickle shape and reduces the cells' oxygen-carrying capacity, thus setting the stage for the disease.