The Award of the Nobel Prize in Medicine to Dr. Hans FischerAuthor(s): P. A. LeveneSource: The Scientific Monthly, Vol. 32, No. 2 (Feb., 1931), pp. 190-192Published by: American Association for the Advancement of ScienceStable URL: http://www.jstor.org/stable/15002 .

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190 THE SCIENTIFIC MONTHLY

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THE PROGRESS OF SCIENCE 191

mT41.' AUYAPr) OTF THE M NOREL PRIZE IN MEDICINE TO DR. HANS FISCHER

THE question which arises in the mind of the general public--and the general public includes everybody except closely related specialists-when a scientist is extolled by the award of a Nobel Prize is, What benefit will mankind derive from the work which is thus singled out? The practical benefit, however, is not the standard of rating of scientific attainment unless the term includes the satisfaction of the curiosities of the human mind. The standard for rating a scientific work is based on the aims of the given branch of science. Chemistry is a broad science composed of many branches, each having its own tasks, each with its own history. The branch of chemistry to which the contributions of Hans Fischer belong is named "Or- ganic Chemistry." Its aim is the study of the architecture of substances of plant or animal origin. It is one of the oldest fields of human endeavor, yet it won the rank of a rational science only in the second half of the last century when it evolved its own theory and its own aims. Until that time the contri- butions of organic chemistry were of an empirical character. The great contri- bution of organic chemistry of the nine- teenth century was the evolution of theory. If the Nobel Prize had then existed, it should have been awarded to Wbhler, Dumas, Laurent and Gerhardt, Kolbe and Frankland, Cooper and Kekule-not for work on the molecular architecture but for devising ways by which the architecture became discover- able. The possessionr of the theory then made it possible to proceed with the original aim of organic chemistry. Indeed, so true; is the theory that for nearly three quarters of a century it led to one discovery after another which were crowned with Nobel prizes. Suffice it to mention the names of Emil Fischer in connection with the molecular struc- ture of sugars and of uric acid; v. Beyer

with the structure of indigo; Willstiitter with the structure of chlorophyll; Wie- land with the structure of bile acids; Windaus with the structure of cho- lesterol. To this list now is added the name of Hans Fischer in connection with the structure of hemoglobin.

The history of hemoglobin is a very long one. The substance was discovered in 1849 by a biologist, Leydig, who ob- served red crystals in venous blood ex- amined microscopically. Later observ- ers who prepared the crystals, not in microscopic but in considerable quanti- ties, were sceptical as to the origin of the color and were inclined to attribute the color to a contaminating substance. In 1862 Hoppe-Seyler, having resorted to the spectroscope for the analysis of the substance, established its individual- ity and introduced the name "hemal- globin." Hoppe-Seyler also recognized that hemoglobin was a complex protein which could be decomposed into a color- less protein and into a component re- sponsible for the color. In fact, the colored component had been known since 1853 when Teichmann described the blood crystals which are nothing else but the colored component of hemo- globin combined with chlorine. The function of hemoglobin in the organism is to transport to the tissues the oxygen required by them for their respiration; in other words, to permit them to de- velop the energy required for their re- spective functions. Hemoglobin, or rather its colored component, hematin, constantly undergoes decomposition and its supply constantly needs replenish- ing. It is calculated that every two and a half months the total hematin supply of the human organism is en- tirely renewed. The place of destruc- tion of hematin is in the liver and the useless product of its decomposition is the so-called bile pigment, bilirubine. The existence of a chemical relationship

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192 THE SCIENTIFIC MONTHLY

between the two substances was long known to physiologists, but the exaci nature of the relationship was in need of explanation. In course of time it was found that substances related to hematin have a wide distribution in living cellk of animal and plant origin and also in non-cellular tissues of all forms of life. The nearest relative of hematin is the chlorophyll present in all green plants.

Thus it is seen that the problem of the structure of hematin and re- lated substances had engaged the in- terest of biologists and of chemists for a very long time and, indeed, to Willstatter the Nobel Prize had already been awarded for his contribu- tion to the chemistry of chlorophyll and Willstiitter already had suggested a theory of the structure of hematin. Kuster, in 1912, advanced a theory of structure of hematin which is not much different from the one evolved by Hans Fischer. The question here again arises as to the unusual merit of the work of the latter. The answer is found in the writings of Hans Fischer himself. The colored component of hemoglobin as first crystallized has the composition C34H32N404F3Cl, hence it consists of 76 atoms. A theory of structure of the substance must represent such an ar- rangement of the atoms with respect to each other which expresses all its prop- erties and all its transformations. Often, however, several closely related arrangements may express sufficiently well the properties of a substance and the selection of the true may present great difficulties. In discussing his own speculations as well as those of other workers, Hans Fischer repeatedly em- phasized that the truth of the theory can be demonstrated only by synthesis and such a proof has finally been fur- nished by himself. To realize the mag- nitude of the achievement it is necessary to understand that the porphyrine (the iron and chlorine free part) of hemin

consists of four pyrrolnuclei (not all of identical structure) each consisting of a ring structure containing 4 carbon atoms and 1 nitrogeni. These four uniits are combined by links of a carbon atoim into a larger ring containing in all 20 carboni atomns. The remainder of the carbon atomis, 14 in number, have to be distributed as side chains of the four pyrrolnuclei. Information as to this distribution was obtained to some extent by the process of cleavage which led to the formation of the hemapyrrol bases and hemapyrrol acids. From the theory of the structure of these fragmiients by speculation, the molecule of hemin has been reconstructed. Hans Fischer, how- ever, reconstructed the molecule of hemin experimentally step by step, first contributing much to the knowledge of the pyrrolderivates, then comnbining two pyrrolnuclei through a carbon link into a single complex, and, furthermore, linking these complexes into such as coin- tain the skeleton of the porphyrines consisting of a system of four pyrrol- nuclei as it oceurs in hemin. Finally, he succeeded in producing in the labora-- tory hemin as it occurs in nature.

Hans Fischer began his work in 1911 with a study of bilirubine, the bile pig-- ment, and its relationship to urobiline, the urine pigment. The work was be- gun at the suggestion of Professor Fried- rich Muiller, the great clinician, whose assistant Fischer then was. One could scarcely have predicted, at that time, that this mnodest beginning would lead to the elucidation of an extensive class of pigments oecurring in all forms of life with a promise of further dis- coveries. It must be emphasized that ingenuity of mind and virtuosity of technique alone were not sufficient to accomplish the work of Fischer. It re- quired, in addition, the gift of leader- ship and organization.

P. A. LEVENE

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