- In full:
- Emil Hermann Fischer
- Born:
- Oct. 9, 1852, Euskirchen, Prussia [Ger.]
- Died:
- July 15, 1919, Berlin, Ger. (aged 66)
- Awards And Honors:
- Nobel Prize (1902)
- Subjects Of Study:
- carbohydrate
- enzyme
- monosaccharide
- protein
- purine
Emil Fischer
-
Who was Emil Fischer?
Emil Fischer (1852ā1919) was a German chemist renowned for his work with sugars and purines, earning the Nobel Prize in Chemistry in 1902. His research elucidated the structures of compounds like uric acid, xanthine, and caffeine, linking them to a nitrogenous base he termed purine.
Fischer's study of sugars involved their interaction with phenylhydrazine, leading him to understand their spatial isomerism, explained by the tetrahedral carbon atom theory of Jacobus Henricus van 't Hoff. Later, at the University of Berlin, Fischer researched enzymes and proteins, proposing that amino acids in proteins are linked by peptide bonds. He synthesized polypeptides, demonstrating their breakdown by enzymes like natural proteins.
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What field of science did Emil Fischer work in?
Emil Fischer, a German chemist, was awarded the Nobel Prize in 1902 for his work in chemistry. His work focused on investigations of sugars and purine groups of substances. Fischer studied chemistry at the University of Bonn and later earned a doctorate under Adolph von Baeyer in 1874. Fischer also devised the Fischer projection, a method for representing the three-dimensional structures of molecules on paper.
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What is Emil Fischer famous for discovering or studying?
Emil Fischer, a German chemist, received the Nobel Prize in Chemistry in 1902 for his work with sugars and purines. Fischer discovered phenylhydrazine in 1875 and determined the structure of rosaniline dyes with his cousin Otto.
Later, Fischer extensively studied sugars, purines, enzymes, and proteins. His research on sugar digestion by yeast led him to conclude that enzymes have a specific spatial orientation to interact with sugar molecules. Fischer also identified peptide bonds in proteins and synthesized long chains of amino acids to create protein-like substances. In 1899, he proposed the "key-lock" hypothesis, explaining the specificity of enzymes. Additionally, Fischer Projections are a method of representing 3D molecular structures on paper, particularly useful for depicting isomers of sugars.
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How did Emil Fischerās work help scientists understand sugars?
Emil Fischer's work significantly advanced the understanding of sugars through his innovative use of classical chemical methods. His research aimed to determine the chemical structure and configuration of isomeric sugars like glucose, galactose, fructose, and sorbose.
Fischer discovered that sugars react with phenylhydrazine to form osazones, which are crystalline compounds that are easy to purify. He recognized that these sugars were spatial isomers, differentiated by the tetrahedral carbon atom theory proposed by Jacobus Henricus van 't Hoff. Fischer's study of the digestion of sugars by yeast led him to conclude that enzymes have a specific spatial orientation to interact with sugar molecules. His work laid the groundwork for understanding the spatial properties of molecules, particularly in the context of sugars.
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What was Emil Fischerās contribution to the study of proteins and enzymes?
Emil Fischer significantly contributed to the study of enzymes and proteins. His research on sugars showed that enzymes have a specific spatial orientation to react with sugar molecules, leading to the "key-lock" hypothesis, explaining enzyme specificity. Fischer proposed that proteins are composed of amino acids linked by peptide bonds. He synthesized long chains of amino acids held together by peptide bonds, creating protein-like substances. In 1907, he created a polypeptide with 18 amino acids and showed that enzymes could break it down like a natural protein.
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Which major award did Emil Fischer receive, and why was it important?
Emil Fischer received the Nobel Prize for Chemistry in 1902 for his work with sugars and purines. His research on purines, beginning in 1882, demonstrated that compounds like uric acid and caffeine shared a common nitrogen-containing base, which he named purine. Later, his study of sugars, particularly their reaction with phenylhydrazine, helped to understand their structure and isomerism. This was key to differentiating the known isomers and synthesizing nine more, using spatial arrangements around carbon atoms. His work laid the groundwork for understanding the structure and function of enzymes and proteins, contributing significantly to biochemistry.
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Emil Fischer (born Oct. 9, 1852, Euskirchen, Prussia [Ger.]ādied July 15, 1919, Berlin, Ger.) was a German chemist who was awarded the 1902 Nobel Prize for Chemistry in recognition of his investigations of the sugar and purine groups of substances.
Education and early career
Fischer was the eighth child and only surviving son of Laurenz Fischer and Julie Fischer. Laurenz Fischer was a local businessman and entrepreneur. Emil Fischer studied chemistry at the University of Bonn, where he attended the lectures of August Kekule, but he was disappointed with the practical instruction of analytical chemistry at the school. With his cousin Otto Fischer, he transferred in 1872 to the University of Strasbourg, where Adolph von Baeyer had recently been appointed as director of the chemical institute. Fischer earned a doctorate under Baeyer in 1874, and Baeyer chose Fischer to be a private assistant in his research laboratory. Baeyer retained Fischer as an assistant when he moved to the University of Munich in 1875 and soon recommended Fischer for the position of associate professor in charge of the analytical division. While at Strasbourg and Munich, Fischer quickly earned a reputation as an excellent organic chemist. He discovered the compound phenylhydrazine in 1875, and with his cousin Otto he established the structure of the rosaniline dyes discovered earlier by the German chemist August Wilhelm von Hofmann. On the basis of his work in organic chemistry, Fischer was appointed director of the chemical institutes at the provincial Bavarian universities of Erlangen (1882) and Würzburg (1885).
Purine and sugar research
After leaving Baeyerās laboratory, Fischer applied the classical chemical methods of organic chemistry to establish the structure of biological compounds such as sugars, purines, and proteins. Fischer began research on the purines in 1882, and during the next 17 years he showed that uric acid, xanthine, caffeine, and other natural compounds were all related to a nitrogen-containing base with a bicyclic structure that he named purine.
In 1884 Fischer began a long study to establish the chemical structure and configuration of the known isomeric sugarsāglucose, galactose, fructose, and sorboseāwith the goal of ascertaining the source of their isomerism. The key to this study was the reaction of the sugars with phenylhydrazine. The sugars themselves had been difficult to purify and characterize, but they reacted with phenylhydrazine (an organic compound commonly used in the synthesis of indole) to give osazones that were highly crystalline, easily purified compounds. Fischer soon realized that these sugars were spatial isomers and could be differentiated by applying the theory of the tetrahedral carbon atom, first proposed in 1874 by the Dutch chemist Jacobus Henricus van āt Hoff. Fischer recognized that the known isomers of glucose represented only 4 out of the 16 possible spatial isomers predicted by van āt Hoffās theory. Using the osazone derivatives and synthetic techniques for the sugars developed by the German chemists Bernhard Tollens and Heinrich Kiliani, Fischer was able not only to differentiate the known isomers but to synthesize nine of the predicted isomers.
Enzyme and protein research
In 1892, largely on the basis of his extensive study of sugars and purines, Fischer was chosen to succeed Hofmann as professor of chemistry at the University of Berlin, at the time the largest and most prestigious chemical institute in Germany. Under his direction, the chemical institute in Berlin became one of the most flourishing sites for all areas of chemistry in the world. He directed the research of hundreds of pupils and associates from Europe, North America, and Japan.
In Berlin, Fischerās research moved to the study of enzymes and proteins. Fischerās extensive study of the sugars included an investigation of their digestion by yeast, and he found that of the known stereoisomers of glucose, only a few were capable of being digested by the enzymes in yeast. Because these isomers differed only in their spatial properties, Fischer concluded that the enzyme in yeast must also have a specific spatial orientation to receive the sugar molecule and react with it.
Thus, Fischer also became involved in establishing the chemical structure of enzymes and proteins. Proteins were known to be composed of amino acids, but Fischer specifically proposed that the amino acids in proteins were linked together by amide bonds, called peptide bonds by Fischer, who established the presence of this class of molecules in proteins by developing synthetic methods for creating long chains of amino acids held together by peptide bonds to make proteinlike substances. In 1907 he created a polypeptide with 18 amino acids and showed that it could be broken down by enzymes in the same way as a natural protein.
Honours and final years
On the basis of his work in purines and sugars, Fischer received the second Nobel Prize for Chemistry, the first organic chemist to receive the honour. While in Berlin, Fischer also became active in the promotion of chemistry and science in Germany. He was instrumental in establishing the Kaiser Wilhelm Society and its related institutes for chemistry and physics in 1911, and he took part in organizing the production of chemicals in Germany during World War I. Sent into a depression by the human and material costs of the war (including the loss of two of his three sons), as well as a diagnosis of intestinal cancer, he apparently committed suicide in 1919.