Theorell, Hugo

Theorell, Hugo, Heme-Linked Groups and Mode of Action of Some... 

Riboflavin was first isolated from whey in 1879 by Blyth, and the structure was determined by Kuhn and coworkers in 1933. For the structure determination, this group isolated 30 mg of pure riboflavin from the whites of about 10,000 eggs. The discovery of the actions of riboflavin in biological systems arose from the work of Otto Warburg in Germany and Hugo Theorell in Sweden, both of whom identified yellow substances bound to a yeast enzyme involved in the oxidation of pyridine nucleotides. Theorell showed that riboflavin 5 -phosphate was the source of the yellow color in this old yellow enzyme. By 1938, Warburg had identified FAD, the second common form of riboflavin, as the coenzyme in D-amino acid oxidase, another yellow protein. Riboflavin deficiencies are not at all common. Humans require only about 2 mg per day, and the vitamin is prevalent in many foods. This vitamin... 

Theorell, Axel Hugo Theodor (1903-1982) Swedish Biochemist Axel Hugo Theodor Theorell was born at Linkoping, Sweden, on July 6, 1903, to Thure Theorell, surgeon major to the First Life Grenadiers practicing medicine in Linkoping, and his wife, Ar-mida Bill. 

When Hugo Theorell worked in Warburg s laboratory between 1933 and 1935, he became familiar with that yellow enzyme his further work on that protein was part of the achievements for which he was awarded the Nobel Prize in 1951. According to a reference in the Encyclopedia Britannica, Warburg had been shortlisted in 1944 for a second Nobel Prize based on his work on flavoproteins, but he could not receive it due to the political situation in Nazi Germany however, the authenticity of that report is doubtful. ... 

The respiratory cytochrome c found in the mitochondria of all eukaryotes is a protein with one heme c (Fig. 1) and 103-113 amino acids in a single polypeptide chain with no disulfide crosslinks. It is small and easily extracted from ruptured mitochondria, in contrast to the other protein components of the respiratory chain, which are larger and generally membrane-bound. For this reason, cytochrome c was the first cytochrome to be studied extensively, and has received the most attention from biochemists. The story of its discovery by MacMunn in 1884, its violent rejection by chemist and editor Hoppe-Seyler, subsequent neglect until rediscovered by David Keilin in 1925, and extensive characterization by Hugo Theorell and his school, is a familiar story which need not be repeated here. Good accounts of this history are to be found in reviews... 

Edman, Pehr Victor, 1916-1977 (pp. 118,240, Plate 15) born in Stockholm in 1916, matriculation examination in 1935, studied medicine at the Karolinska Institute Medical School in Stockholm from 1935, Bachelor of Medicine in 1938, graduation as a physician in 1946. Concurrently with his studies in medicine he started his training in biochemistry with Erik Jorpes, for a short time also with Hugo Theorell, and soon started a project on angiotensin that led to a MD thesis. Then he widened his experience in protein chemistry during one year at the Rockefeller Institute in Princeton with Northrop and Kunitz (crystallization of proteolytic enzymes). On his return to Sweden, Edman was awarded an associate professorship in Lund in 1947 where he conducted his stepwise peptide degradation work (p. 118) between 1950 and 1956. In 1957 Pehr Edman accepted an offer to be Director of Research at St. Vincent s School of Medical Research in Melbourne, Australia, where he remained for 15 years, during which the work on an automated sequence analyzer was finished in 1967. From 1972 until his death from a brain tumor in 1977 he was Director of the Department of Protein Chemistry of the Max-Planck-Institute for Biochemistry in Martinsried near Munich. 

Swedish biochemist Hugo Theorell (1903-82) isolates the muscle protein myoglobin. 

Part of this essay is excerpted from the Nobel Lecture by Hugo Theorell The Nature and Mode of Action of Oxidation Enzymes, The Nobel Foundation, Stockholm, 1955). 

Fig. 2. Madrid, 1969. Left to right David Nachmansohn, Fritz Lipmann, Hugo Theorell, Severe Ochoa, Ernst Chain, Zacharias Dische, Carl Cori. 

Hugo Theorell, Biochemical Department, Medical Nobel Institute, Stockholm, Sweden... 

The term flavin stands for the yellow redox-active subgroup of the first coenzyme ever to be elucidated in terms of molecular structure. The heroic period of redox-enzymology of the early thirties ended in Hugo Theorell s 172—175) description of the first enzyme ever to be split reversibly to yield coenzyme and apoprotein. This was the NADPH-... 

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