Hugo Theorell

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Hugo Theorell, a Swedish-born scientist, was a Nobel laureate. He was awarded the Nobel Prize in Physiology or Medicine for his seminal work on oxidation enzymes. His previous research on the role of lipids demonstrated that lipids play a critical role in lowering the erythrocyte sedimentation rate, or ESR. He is credited with discovering red muscle proteins such as crystalline myoglobin. He referred to this protein as the oxygen carrier in the muscle area. His exhaustive research defined the chemical structure of a yellow-colored yeast enzyme. Additionally, he carried out extensive research on the chemical structure of cytochrome. Apart from that, he investigated the relationship between cytochrom and the heme nucleus. His pioneering research established the mechanism by which ADH enzymes degrade alcohol in the kidney. He made significant contributions to the isolation of enzymes found in milk, such as lactoperoxidase. Later in life, he conducted research on the crystallization of an enzyme from a horse’s liver. He also continued his research into ethyl alcohol. Hugo’s development of a blood alcohol test to detect drunk drivers is one of his most significant contributions. He received several honorary doctorates from seven prestigious universities in locations such as Paris, Pennsylvania, and elsewhere.

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Childhood & Adolescence

Hugo Theorell was born in Linkoping, Sweden, the son of Thure Theorell, a surgeon-major with the Linkoping First Life Grenadiers, and Armida Bill. Hugo spent nine years at Linkoping’s State Secondary School.

On May 23, 1921, he passed the school’s matriculation examination. He was admitted to the Karolinska Institute in the same year to study medicine. He earned a Bachelor of Medicine degree in 1924.

Following a brief period, he began working as an assistant at Stockholm’s Institute of Medical Chemistry. He worked as a temporary associate professor at this institute from 1928 to 1929.

Following that, he spent three months at the Pasteur Institute in Paris studying bacteriology under Professor Calmette. In 1930, he earned his M.D. His thesis was on the lipids found in blood plasma.

Career of Hugo

After earning his M.D., he worked at the Karolinska Institute as a lecturer in psychological chemistry. Hugo discovered the presence of crystalline myoglobin in 1931 while conducting research at Svedberg’s Institute of Physical Chemistry in Uppsala, Sweden.

The following year, he joined the University of Uppsala as an associate professor of medical and psychological chemistry. He later worked as a Rockefeller Fellow in Otto Warburg’s Berlin-Dahlem laboratory from 1933 to 1935.

He was then conducting research on oxidation enzymes. In 1934, he purified and crystallized a yellow-colored enzyme found in yeast using his own electrophoretic methods.

Additionally, he isolated lactoflavin, an enzyme pigment, from the colorless protein carrier. His research established that the lactoflavin component was a type of protein.

He named the substance flavin mononucleotide based on its chemical structure. In 1937, he was appointed director of the Nobel Medical Institute’s Biochemical Department in Stockholm.

He began his research on the structure of cytochrome and its relationship to the heme nucleus in 1938. He served as Secretary of the Swedish Medical Society from 1940 to 1946.

In 1941, he was kept busy by research on the relationship between iron and cytochrome. He collaborated with Anders Ehrenberg on research into the structure of the cytochrome c molecule. Their work established that the cytochrome c core contains an iron atom.

Additionally, their work pioneered the concept of embedded heme. According to this theory, cytochrome c’s core is surrounded by helical peptide chains to protect its iron atom from oxidizing agents. He also built a model of this central section to illustrate his theory.

He was a member of the Swedish Society for Medical Research from 1942 to 1950. He crystallized a horseradish peroxidase in collaboration with his coworkers.

In 1943, they isolated lactoperoxidase, a type of enzyme found in milk. He served as Chairman of the Swedish Medical Society from 1947 to 1948.

Additionally, he served as Chairman of the Swedish Chemists Association from 1947 to 1949. He was instrumental in crystallizing an enzyme from a horse’s liver in 1948.

In 1950, his research determined the dehydrogenase enzyme’s velocity. He served on the State Research Council for the Natural Sciences from 1950 to 1954.

He continued his research into the mechanism of action of alcohol dehydrogenases at that time. Apart from his research, he served as the chief editor of “Nordisk Medicin,” a journal founded in 1954.

His pioneering research established that the liver enzyme oxidizes alcohol and converts it to aldehyde, while the yeast enzyme plays a critical role in reducing aldehyde to alcohol.

His subsequent research focused on ethyl alcohol. In 1957, he was elected as a Foreign Associate of the National Academy of Sciences in Washington. He was elected a Foreign Member of the Royal Society in 1959.

He served as president of the Swedish Academy of Sciences from 1967 to 1968. He served as president of the International Union of Biochemists from 1967 to 1973.

Personal History and Legacies

Elin Margit Elilsabeth Alenius Theorell was his wife in 1931. Elin Margit was a professional pianist. Eva Kristina Theorell was their daughter, and Klas Thure Gabriel, Henning Hugo, and Per Gunnar Tores Theorell were their sons. Hugo was assassinated in Stockholm.

Estimated Net Worth

The net worth of Hugo is unknown.

Trivia

This eminent Swedish scientist was particularly interested in music and was a member of the Swedish Royal Academy of Music. Additionally, he was well-known as a gifted violinist.