Edmond H. Fischer

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Edmond H. Fischer
Born (1920-04-06) April 6, 1920 (age 94)
Shanghai, China
Doctoral students Edwin G. Krebs
Known for Phosphorylation
Notable awards Nobel Prize in Physiology or Medicine in 1992

Edmond Henri Fischer (born April 6, 1920) is a Swiss American biochemist. He and his collaborator Edwin G. Krebs were awarded the Nobel Prize in Physiology or Medicine in 1992 for describing how reversible phosphorylation works as a switch to activate proteins and regulate various cellular processes.[1] Since 2007, he has been the Honorary President of the World Cultural Council.[2]

Early life[edit]

Fischer was born in Shanghai, China. His mother, Renée Tapernoux, was born in France, and his father, Oscar Fischer, was born in Austria.[3] Fischer's maternal grandfather founded the "Courrier de Chine" in Shanghai, which is the first newspaper published in French in China; he also helped to establish "l'Ecole Municipale Française" in Shanghai, where Fischer attended primary school.[4]

Switzerland[edit]

At age 7 he and his two older brothers were sent to the Swiss boarding school La Châtaigneraie, near the home town of his mother, Renée Tapernoux, in Vevey. At high school he made a pact with a childhood friend, one of them would become a doctor and the other a scientist and then they could cure the ills of the world. While at high school Fischer was admitted to the Geneva Conservatory of Music, he also considered becoming a professional musician.

At the completion of high school Fischer wanted to study microbiology, however he was advised to study chemistry. He studied at the University of Geneva during World War II, he enjoyed organic chemistry and also studied biology. He completed a PhD in organic chemistry under the supervision of Kurt H. Meyer, who worked on the structure of polysaccharides, and the enzymes needed for their synthesis and breakdown. Fischer worked on alpha-amylase.

Reversible protein phosphorylation

USA[edit]

Fischer went to the United States in 1950 for post-doctoral research. He was supposed to take up a position at Caltech, but he was also, unexpectedly, offered a position at the University of Washington, Seattle. Seattle reminded Fischer and his wife of Switzerland so they chose to settle there.

Research[edit]

Six months after his arrival in Seattle, Fischer began collaborating with Ed Krebs. They worked on glycogen phosphorylase; Krebs and Fischer defined a series of reactions leading to the activation/inactivation of this enzyme as triggered by hormones and calcium, and in the process discovering reversible protein phosphorylation.

Explained simply reversible protein phosphorylation works like this: a protein kinase moves a phosphate group from adenosine triphosphate (ATP) to a protein. The shape and the function of the protein is altered enabling it to take part in some biological process. When the protein has completed its role a protein phosphatase removes the phosphate and the protein reverts to its original state. This cycle takes place to control an enormous number of metabolic processes.[5][6]

For the key discovery of reversible protein phosphorylation, Fischer and Krebs were awarded the Nobel Prize for Physiology or Medicine in 1992.

Through his career Fischer's research continued to look at the role reversible protein phosphorylation played in a variety of cellular processes.

Notes[edit]

  1. ^ "The Nobel Prize in Physiology or Medicine 1992 Press Release". Nobel Assembly at Karolinska Institutet. Retrieved August 21, 2013. 
  2. ^ Almada López, Carlos. "World Cultural Council 24th Award Ceremony, Closing Remarks" (in Spanish). Retrieved August 21, 2013. 
  3. ^ http://www.bookrags.com/biography/edmond-h-fischer-wap/
  4. ^ "Edmond H. Fischer - Biographical". nobelprize.org. Retrieved August 21, 2013. 
  5. ^ Fischer, E H; Krebs, E G (1966), "Relationship of structure to function of muscle phosphorylase.", Fed. Proc. 25 (5): 1511–20, PMID 5332191 
  6. ^ KREBS, E G; FISCHER, E H (1964), "PHOSPHORYLASE AND RELATED ENZYMES OF GLYCOGEN METABOLISM.", Vitam. Horm. 22: 399–410, doi:10.1016/S0083-6729(08)60345-3, PMID 14284112 

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