Hugo Theorell Biography
Nobel laureate Hugo Theorell was a scientist of Swedish origin. He received Nobel Prize in Physiology of Medicine for his important discoveries of oxidation enzymes. His earlier research works regarding the role of lipids showed that lipids have a significant role in reducing erythrocyte sedimentation rate or ESR. He is credited for discovering proteins like crystalline myoglobin, found in red muscle. He described this protein as the carrier of oxygen in muscle area. His extensive study defined the chemical structure of yellow colored enzyme found in yeast. He also conducted detail research on the chemical structure of cytochrome. Apart from that, he studied the link of cytochrom with heme nucleus. His innovative research showed the working process of ADH enzymes in breaking down alcohol in kidney. He had an important contribution regarding the isolation of enzymes like lactoperoxidase, found in milk. In later period of his life, he researched to crystallize an enzyme from horse’s liver. He also pursued his study on ethyl alcohol .One of the most important discoveries of Hugo includes his development of blood alcohol test to check drunk drivers. He was the recipient of several honorary doctorates from seven prestigious universities of places like Paris, Pennsylvania and so on.
- Born in Linkoping, Sweden, Hugo Theorell was the son of Thure Theorell, a surgeon-major to the First Life Grenadiers in Linkoping and Armida Bill. Hugo attended a State Secondary School in Linkoping for nine years.
- He cleared his matriculation examination from that school on May 23, 1921. In the same year, he took admission at the Karolinska Institute to study medicine. In 1924, he graduated as a Bachelor of Medicine.
- After a brief period, he started working as an assistant at the Institute of Medical Chemistry at Stockholm. From 1928 to 1929, he served as a temporary associate professor at this institute.
- After that, he studied bacteriology under Professor Calmette for three months at the Pasteur Institute in Paris. He became an M.D. in 1930. The subject of his thesis was the lipids of the blood plasma.
- After completing his M.D., he worked as a lecturer in psychological chemistry at the Karolinska Institute. It was Hugo who for the first time noticed the presence of crystalline myoglobin while pursuing research works in Svedberg’s Institute of Physical Chemistry in Uppsala, Sweden in 1931.
- In the following year, he worked as associate professor of medical and psychological chemistry at the University of Uppsala. Later, from 1933 to 1935, he worked as a Rockefeller Fellow in the laboratory of Otto Warburg at Berlin-Dahlem.
- At that time, he pursued research on oxidation enzymes. In 1934, with the application of his own electrophoretic methods, he purified and crystallized a yellow colored enzyme found in yeast.
- Moreover, he separated lactoflavin, a pigment part of that enzyme from the colorless protein carrier. His research established the fact that the portion of lactoflavin was a type of protein.
- Based on its chemical structure, he named the substance as flavin mononucleotide. In 1937, he acted as the director of the Biochemical Department of the Nobel Medical Institute in Stockholm.
- In 1938, he conducted research on the structure of cytochrome and its relation with heme nucleus. From 1940 to 1946, he acted as the Secretary of Swedish Medical Society.
- In 1941, the research work on the relation of iron with cytochrome kept him busy. His joint research work with Anders Ehrenberg was about the structure of the cytochrome c molecule. Their work proved that the centre of the cytochrome c contains an iron atom.
- Besides this, their work introduced the theory of embedded heme. According to this theory, the core portion of cytochrome c is surrounded by helical peptide chains to protect its iron atom from oxidized agents. He also constructed a model of this centre part to provide a clear idea about his theory.
- From 1942 to 1950, he served as a member of the Swedish Society for Medical Research. In association with his co-researchers, he crystallized a peroxidase of horseradish.
- In 1943, their research work resulted in the isolation of lactoperoxidase, a type of enzyme from milk. From 1947 to 1948, he was the Chairman of the Swedish Medical Society.
- Moreover, he acted as the Chairman of the Association of Swedish Chemists from 1947 to 1949. In 1948, he played a vital role in crystallizing an enzyme from horse’s liver.
- In 1950, his research work determined the velocity of the liver dehydrogenase. From 1950 to 1954, he was a member of the State Research Council for the Natural Sciences.
- At that time, he continued research on the working process of the alcohol dehydrogenases. Besides research works, he also acted as the chief editor of “Nordisk Medicin”, a journal from 1954.
- His innovative research work showed that the enzyme secreted from liver oxidizes alcohol and transforms it into aldehyde and the yeast enzyme plays a key role in reducing aldehyde to alcohol.
- His next research work was on ethyl alcohol. In 1957, the National Academy of Sciences in Washington elected him as its Foreign Associate. In 1959, he became a Foreign Member of the Royal Society.
- From 1967 to 1968, he was the president of the Swedish Academy of Sciences. From 1967 to 1973, he played the role of the president of the International Union of Biochemists.
- He married Elin Margit Elilsabeth Alenius Theorell in 1931. Elin Margit was a pianist by profession. They had a daughter, Eva Kristina Theorell and three sons whose names were Klas Thure Gabriel, Henning Hugo and Per Gunnar Tores Theorell. Hugo passed away in Stockholm.
- This renowned scientist of Swedish origin had a special interest in music and was a member of the Swedish Royal Academy of music. Moreover, he was also well known as a talented violinist.
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