Emil Fischers Life

Emil studied three years with a private tutor and then attended the local public school for four years. This was followed by two years of schooling at Wetzler and two more at the gymnasium in Bonn. He passed his final examination in 1869 at the latter institution with great distinction. 

There was disagreement about choosing a career. His father wanted to maintain the family tradition and to train Emil to become a successor in business. Emil preferred natural science, mathematics, and especially physics. Emil s trial period in business was a failure. HSs 

The start of Emil s higher education had to be delayed because the eighteen-year-old youth had to recover from gastric catarrh before he could leave home. The father sent Emil to the University of Bonn in 1871 to study chemistiy. At Bonn he attended the lectures of Kekule, Engelba, and Zincke. Emil still had a strong interest in physics, and only the peraistent persuasion of his cousin and fellow student, Otto Fischer (1852-1932) prevented him from deserting chemistry. 

Emil and his cousin transferred to Strasbourg in the fall of 1872. Studying under Rose, Fischer became acquainted with Bunsen s methods for the analysis of water. This experience proved useful when the young man did analsitical work for the town of Colmar. 

Emil devoted most of his time to chemistry during his seven semesters at Strasbourg. However, he also studied 

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Of all the monosaccharides d (+) glucose is the best known most important and most abundant Its formation from carbon dioxide water and sunlight is the central theme of photosynthesis Carbohydrate formation by photosynthesis is estimated to be on the order of 10 tons per year a source of stored energy utilized directly or indi rectly by all higher forms of life on the planet Glucose was isolated from raisins m 1747 and by hydrolysis of starch m 1811 Its structure was determined in work culmi nating m 1900 by Emil Fischer... 

In the autumn of 1907, he started to study chemistry at the Institute chaired by Adolf von Baeyer at the University of Munich, where he passed the first Verband s examination after three semesters. In 1909, he continued his studies at the University of Berlin, gaining his doctorate in 1911 under Emil Fischer. The subject of his doctoral dissertation was Syntheses of Certain New Glucosides. The tremendous personality of Emil Fischer left its mark on Helferich for the rest of his life. In conversation with Helferich, one was often aware of the great veneration he always felt for his tutor and mentor. 

He was convinced that optical activity is a peculiarity of life and, therefore, his view was directed toward asymmetry at a cellular level rather than at the molecular level developed by Emil Fischer. 

He never gave unbridled rein to his synthetic efforts, nor did he fall into the temptation of purposeless synthesis. He always remained a true scientist—a student of nature.. . . This great individual was a man of inflexible veracity and simplicity.. . . Emil Fischer s life was based on responsibility a responsibilityfor the austerity andpurity of his work and its aims, responsibility for the university as an important organ of our cultural and economic life, and responsibility for each of his students. 

When Emil Fischer died in August, 1919, at the age of 67 years, he bequeathed a life-work of rare comprehensiveness. He had contributed greatly to our knowledge of the material world, and especially to that of organisms. He refocused the thinking in organic chemistry back to its starting point, the world of animated Nature. 

The life and work of one of the greatest carbohydrate scientists of our time, Raymond U. Lemieux, is recalled here in a sensitive account by Bundle (Edmonton). During a remarkably productive career extending over more than half a century, Lemieux pioneered the application of NMR spectroscopy in chemistry, developed rational approaches for glycosidic coupling, made major contributions to our understanding of three-dimensional carbohydrate structures and protein binding, and made important contributions in the biomedical area. His own articles in these Advances include the chemistry of streptomycin in Volume 3, the mechanisms of replacement reactions in Volume 9, and in Volume 50 a consideration of Emil Fischer s lock and key concept of enzyme specificity. 

What do proteins look like Although Emil Fischer showed that they were made of amino acids, the details of their structures were unknown. Their size put them below the reach of even electron microscopy, yet it was becoming clear that proteins were the fundamental machines of life, catalyzing the chemistry and building the structures of the cell. A new technique therefore was needed to study protein structure. 

It is the mode of existence of human society that whatever is discovered/ invented in science/technology, art, and social life will sooner or later be evaluated, mastered, copied/modified/multiplied by others. History is the witness that this is the basic mechanism responsible for development. Just for illustration Emil Fischer (recipient of the 1902 Nobel Prize for chemistry), the pioneer of chemical syntheses that opened the way for the development of carbohydrate and protein chemistry, irreversibly changed the history of a branch of science. Similarly, the van Eyck brothers, who first intentionally used the oil technique, irreversibly changed the history of painting, and so on and so forth. 

Six weeks later, with the emperor in attendance, the Kaiser Wilhelm Society for the Advancement of Sciences rose into life, inflated with the hot air of optimism, ambition, and pride. It represented a unique partnership of imperial sponsorship and private wealth. Private money built the institutes and paid most of their bills, but Prussia paid the salary of each institute director. At the first meeting of the society s governing council, chemist Emil Fischer proclaimed science the true land of unlimited possibilities. When Fischer mentioned, as one example of science s gifts, the capture of nitrogen fertilizer from the air, he saw the emperor nod his head in agreement. 

The kajk-and-key principle formulaled by Emil Fischer as early as Ihc end of the I9i h century has still not lost any of its significance for the life sciences. The basic aspects of ligand-protein interaction may be summarized under the term molecular recognition and concern the specificity as well as stability of ligand binding. 

Leuchs initial elan, fed by intelligence and power of imagination, which after successful (albeit by Emil Fischer inspired) peptide studies launched him into the difficult chemistry of strychnine alkaloids and also into problems of stereochemistry, diminished later, probably under the influence of some decisive inner experience unknown to us. After a while his life was consumed by work in the laboratory he remained unimpressed by the rich cultural and scientific distractions offered by Berlin, that time in its heydays. After 1908 his principal field became strychnine chemistry and related alkaloids 125 of his 178 publications deal with this topic. 

The first Nobel laureate in chemistry (1901) was Jacobus van t Hoff, the veterinarian who visualized three-dimensional carbon. The second Nobel Prize went to Emil Fischer, the guru of natural product identification. The prize was the validation of his work, but not of his life. When three of his four sons were killed in World War I, he committed suicide. 

Mother Nature, generous in supplying an abundance of giant molecules, has not been as generous in the science of her polymers which are complex and present many research difficulties. The difficulties were particularly severe before and durii the life (1852-1919) of Emil Fischer because modem instmments and techniques had not been developed. Nevertheless, Fischer had both the courage to undertake pioneering research on nature s complex macromolecules and the competence needed for success. His creative research comprises an important milestone in man s search for an understanding of polymers. 

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