DAVID EZRA GREEN

August 5, 1910–July 8, 1983

BY HELMUT BEINERT, PAUL K. STUMPF, AND SALIH J. WAKIL

AT THE TIME OF DAVID Green’s death in 1983, Frank Huennekens, one of Green’s postdoctoral fellows, wrote in his personal recollections:

David Green was a remarkable person. Endowed with a keen intellect, an insatiable curiosity about Nature, a vivid imagination and boundless energy, he pursued a career devoted entirely to research. Over a period of four decades he and his colleagues published nearly 700 journal articles and reviews covering a broad spectrum of enzymology and bioenergetics. And, he was the author, co-author or editor of eight books. A legion of postdoctorals and visiting investigators received training in his laboratory. History will surely record that he was one of the giants of 20th-century biochemistry.

Green’s professional career had four distinct periods, during which he explored, developed, and refined the expanding concepts of enzymology. They were his educational experiences at New York University and at Cambridge; his return to the United States to begin his American career for one year at Harvard; his first academic appointment at Columbia College of Physicians and Surgeons in New York City; and finally his selection as codirector of the Institute for Enzyme Research at the University of Wisconsin at Madison, where he remained until his untimely death in 1983. As we will see, Green played a pivotal role in the expanding



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D AV I D E Z R A G R E E N August 5, 1910–July 8, 1983 BY HELMUT BEINERT, PAUL K. STUMPF, AND SALIH J. WAKIL A D AVID G reen’s death in 1983, Frank T T HE T IME O F Huennekens, one of Green’s postdoctoral fellows, wrote in his personal recollections: David Green was a remarkable person. Endowed with a keen intellect, an insatiable curiosity about Nature, a vivid imagination and boundless en- ergy, he pursued a career devoted entirely to research. Over a period of four decades he and his colleagues published nearly 700 journal articles and reviews covering a broad spectrum of enzymology and bioenergetics. And, he was the author, co-author or editor of eight books. A legion of postdoctorals and visiting investigators received training in his laboratory. History will surely record that he was one of the giants of 20th-century biochemistry. Green’s professional career had four distinct periods, during which he explored, developed, and refined the ex- panding concepts of enzymology. They were his educational experiences at New York University and at Cambridge; his return to the United States to begin his American career for one year at Harvard; his first academic appointment at Columbia College of Physicians and Surgeons in New York City; and finally his selection as codirector of the Institute for Enzyme Research at the University of Wisconsin at Madi- son, where he remained until his untimely death in 1983. As we will see, Green played a pivotal role in the expanding 113

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114 BIOGRAPHICAL MEMOIRS frontier of enzymology, not only in the United States but also throughout the world. David Ezra Green was born in Brooklyn, New York, on August 5, 1910. He attended the public school system there and apparently was indifferent to his studies in both his grade-school and high-school days. About his early educa- tion Green explained, “As I look back, school per se ex- erted little influence on me. My friends and my family were the principal catalysts in my development. There was not a single teacher in high school that fired or inspired me, though I respected them all as competent individuals. Curi- ously enough, courses in science did not particularly inter- est me. I hardly know why I avoided them in high school.” Interestingly the Book of Knowledge, an encyclopedia popular during that period, became Green’s bible. Its 20 volumes served as sources of information on subjects ranging from the arts to the sciences. His father loved learning, and it was from him that Green acquired an interest in books, ideas, and self-development. In 1928 Green enrolled in New York University at the Washington Square campus and initially intended to study medicine. After taking the premedical-school curriculum for two years, however, he realized that the field of medi- cine did not interest him. Fortunately he was offered a stu- dent assistantship in the Department of Biology, and there he completed his undergraduate studies in 1931. A very important event was his summer experience at Woods Hole, where he associated with Professor Robert Chambers, the famed cell physiologist, and later with Professor Leonor Michaelis. Apparently the close association with Michaelis inspired Green and aroused his desire to explore more fully the mysteries of biological oxidations. Green received a master’s degree in 1932 at New York

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115 DAVID EZRA GREEN University and left for Cambridge University in England, where his potential talents were nurtured in the fertile soil of the Biochemistry Department led by the famous Sir Frederick Gowland Hopkins. The department was home to some of the greatest biochemists of that period—including David Keilin, Malcolm Dixon, Robin Hill, Joseph and Dor- othy Needham, Judah Quastel, Marjorie Stephenson, Ernest Gale, and Norman Pirie—and was ranked as one of the leading centers of innovative research in the new field of enzymology. Green soon ensconced himself among the department’s many graduate and postgraduate students as the brash young American he was, a character that he did not lose even when made a Beit fellow. Green conducted his graduate studies and research un- der the supervision of Malcolm Dixon, who said of Green’s graduate work, “David threw himself into his research with great enthusiasm, energy, and enterprise. He was full of ideas, which he expressed freely; and although not every- body agreed with all of them, they were always interesting and characterized by freshness and vitality.” In his initial year at Cambridge, Green completed all the research re- quired for his Ph.D. thesis, “The Application of Oxidation- Reduction Potentials to Biological Systems.” Although he received his Ph.D. degree on June 8, 1934, the results of his thesis research had been published in Biochemical Journal in 1933 under the title “The Reduction Potentials of Cys- teine, Glutathione and Glycylcysteine.” During his eight years of research at Cambridge Univer- sity and in collaboration with his colleagues, Green pub- lished an astounding 32 publications in peer-reviewed jour- nals. His scientific genius was best expressed, however, in an eloquent essay titled “Reconstruction of the Chemical Events in Living Cells,” in which he wrote at the age of 27:

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116 BIOGRAPHICAL MEMOIRS The mastering of a particular machine requires not only a knowledge of the component parts, but also the practical ability to take the machine to pieces and reconstruct the original. . . . One may ask with good reason what is the point of imitating the cell with mixtures of the components in test tubes. Is it egotism and vanity on the part of the biochemist or a flair of chemical engineering? The study of mechanism, perforce, must be ex- tremely limited in dealing with intact tissues. The variation of conditions, which is essential to studies of mechanism, must lie within the confines of those tolerated by living material. The biochemist has therefore to resort to the disorganization of the cell in order to puzzle out the mechanisms of reaction. The major discoveries of the mechanisms which cells utilize for their reactions have practically all been made by the analyses of the behav- ior of cell extracts and of enzyme systems. It was also obvious that the talented Green had other thoughts besides his research, in that he became acquainted with Doris Cribb, at the time the director of the design department at the Cambridge School of Art, which ulti- mately led to their marriage on April 16, 1936. In 1940 after the defeat of the British at Dunkirk, the U.S. government recalled all U.S. citizens who were living in Europe. Green, Doris, and their young daughter, Rowena, returned to the United States, where he became a research fellow in the Department of Biochemistry at the Harvard University Medical School. Having refined his skills as an enzymologist at Cambridge, as well as having acquired a magnificent English accent tainted slightly by his Brooklyn years, he began his American career under rather hum- bling circumstances. Green most likely was astounded at the facilities assigned to him at Harvard, when he compared them to those he had enjoyed at Cambridge. There were no cold rooms nearby and no centrifuge in the laboratory. An old Dubosque colo- rimeter was available for colorimetric measurements, and strangely the cupboards in the laboratory were stuffed with an abundance of filter paper in all shapes and sizes. Most

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117 DAVID EZRA GREEN prominently lacking was a key piece of equipment widely used in the 1940s: a Warburg constant volume respirom- eter system. All the cofactors Green needed to conduct his experiments had to be isolated from yeast and from animal tissues. And because his research funds were derived solely from a grant awarded to him by the Ella Sachs Ploetz Foun- dation, he had a rudimentary research team: E. Knox, a bright medical student, and Paul K. Stumpf, a senior at Harvard College. Stumpf reminisced, During my senior year at Harvard (1940-1941), I was required to prepare a research thesis to fulfill the honors requirement in biochemistry. Since I had become interested in enzymes, and since, in 1940, no enzymologist was on the faculty in Cambridge, Massachusetts, I made an appointment to see Professor A. Baird Hastings, at that time the chair of the Department of Biological Chemistry at the Harvard Medical School in Brookline. At the appointed hour, I was ushered into the august and wood-paneled chambers of Hastings and after a brief series of questions, Hastings informed me that he was no longer active in this field but that a “young chap” just back from Cambridge University was downstairs and it would be a worthwhile experi- ence for me to at least meet him. Hastings then took me down to the first floor and we entered a high ceiling, dark laboratory with an enormous stone basin, and a central wooden bench. He introduced me to David Green. After Hastings left, Green asked me a few questions and then in his English accent instructed me to roll up my sleeves and go to work. In this way I began my six-year relation with Green. Limited as Green’s equipment and personnel resources were, he isolated a yeast flavoprotein, purified potato starch phosphorylase, and published his results in the Journal of Biological Chemistry. In 1940 he authored an important book titled Mechanisms of Biological Oxidation, which was published by Cambridge University Press. This 178-page book with its nine chapters had a profound effect on the fledg- ling field of enzymology. With great clarity Green described what was then known about the enzymatic systems involved in oxidation-reduction processes. Equally important was his

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118 BIOGRAPHICAL MEMOIRS essay, “Enzymes and Trace Substances,” published in 1941 in Volume I of the new series titled Advances in Enzymol- ogy. Green wrote in that essay, The thesis which we shall develop in this article is that any substance which occurs in traces in the cell and which is necessary in traces in the diet or medium must be an essential part of some enzyme. We shall define a trace concentration as one where the uppermost limit is less than 5 micrograms per gram dry weight of the cell. . . . The fundamental assumption of the trace substance-enzyme thesis is that there is no rational explanation avail- able of how traces of some substance can exert profound biological activity except in enzymic phenomena. As with his book this essay had a profound effect on the development of the logical explanations of a large number of cofactors that were then already known or were to be discovered during the next decade. With the obvious limit of knowledge in the field in the 1940s Green had trouble explaining the functions of inhibitors and pharmacologi- cally active drugs, as well as of plant and animal hormones. Nevertheless this thesis influenced the directions many bio- chemists took in their researches in the late 1940s and throughout the 1950s. Late in 1941 Green was appointed assistant professor of biochemistry in the Department of Medicine at the Colum- bia College of Physicians and Surgeons in New York City. The department had a distinguished record of research in a broad range of the medical sciences and an excellent group of scientists and clinicians. In addition the building that housed the Department of Medicine also housed an equally distinguished Department of Biochemistry. Green was assigned a small but modern facility that had all the accessory rooms so sorely missing at Harvard. Soon he ac- cumulated sufficient funds to hire a technician and a dish- washer and was able to employ his first and only graduate

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119 DAVID EZRA GREEN student, Paul K. Stumpf, who had already been associated with Green at Harvard. Green was in his element at Columbia, and his research thrived. By 1943 he was able to double his laboratory space by remodeling an adjoining room. Sarah Ratner joined his group at that time and hired as her technician Marian Blanchard. Stumpf occupied the remaining space to con- tinue his collaboration with Green, as well as to carry out his Ph.D. research project on the pyruvic oxidase of Pro- teus vulgaris. In the later years of his Columbia period Luis Leloir and W. Farnsworth Loomis joined Green’s small re- search group. Throughout this period Green kept his desk in his small laboratory, where he administrated the two- room laboratory complex, ordered equipment, carried out all his own experiments, wrote his papers, and met an end- less number of visiting scientists. The Columbia period proved to be an exciting time for Green and his colleagues. With World War II fully under- way and with supplies and equipment at a premium, Green was able to procure ample funding from private sources, such as the Williams-Waterman Fund of the Research Cor- poration, the Rockefeller Foundation, and the Winthrop Chemical Company. His research team published 20 papers on the enzymatic oxidation of amino acids, transamination, and the mechanism of pyruvic acid oxidation. In addition, he supported the construction of an ultrasonic device that was used to disintegrate bacteria, purchased one of the first battery-driven Beckman DU spectrophotometers, and was one of the first biochemists to use the new Waring blender to extract enzymes from tissues. The efficiency and productivity of Green’s laboratory were demonstrated in other ways as well. One time when he needed a supply of milk xanthine oxidase, Green man- aged to obtain 10 liters of raw heavy cream and in the

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120 BIOGRAPHICAL MEMOIRS process of isolating the enzyme produced a large amount of butter as a byproduct. Needless to say, because of short- ages of butter during those war years, the byproduct was rapidly divided and consumed by his collaborators. An excellent scientist, Green had an intuitive sense of designing relevant experiments and a knack for isolating unstable enzyme systems. Enthusiastic, impetuous, and al- ways available for advice and encouragement, he was a rich source of information on all aspects of enzymology. David Nachmanson, Konrad Bloch, David Rittenberg, and David Shemin from the Department of Biochemistry at Columbia frequently sought his advice. Other frequent visitors included Severo Ochoa, Efraim Racker, Herman Kalckar, Fritz Lipmann, Otto Meyerhof, Boris Chain, M. Heidelberger, Karl Meyer, I. C. Gunsalus, W. W. Umbreit, Birgit Vennesland, and many of his former colleagues from Cambridge Uni- versity. Green was largely responsible for the formation of the Enzyme Club, which met monthly at the downtown Co- lumbia University Faculty Club and brought together inves- tigators from the greater New York City area to discuss com- mon interests. This idea caught on throughout the United States and for many years enzyme clubs were established at many urban academic centers. In his last few years at Columbia Green was so successful in isolating and purifying soluble enzymes that he became bored with his successes and expanded his interests into the far more complicated and challenging field of oxida- tive phosphorylation and into multi-enzyme systems, such as those involved in the complete oxidation of pyruvic acid. For these studies Green used insoluble preparations ob- tained each day from rabbit kidneys and named this com- plex mixture of enzyme-bound systems the “cyclophorase system.” Many rabbits were needed to keep a supply of fresh kidneys for this work. The remaining parts of the rabbits

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121 DAVID EZRA GREEN were eagerly sought after by a long line of students and staff who would wait patiently outside Green’s laboratory each morning for their share of fresh meat, presumably to be consumed in the evening as rabbit stew. All the research conducted in Green’s laboratory through- out this period had the imprint of his talent. If he played a key role in the selection of and was an active participant in a research project, he was a coauthor. If on the other hand he merely advised and encouraged the progress of a re- search project carried out by a member of his team, he did not claim coauthorship on the research paper. This policy was to become an established procedure when he became codirector of the Institute for Enzyme Research at the Uni- versity of Wisconsin in Madison. Consequently many very important papers on fatty acid oxidation and fatty acid syn- thesis that were published in the 1950s by researchers at the institute did not carry his name. When the University of Wisconsin decided to organize an enzyme institute, Green, an obvious choice, was selected to be its codirector. He moved from New York to Madison in 1948. Sarah Ratner remained at Columbia. Stumpf joined the School of Public Health at the University of Michigan to investigate virus biochemistry and a year and a half later was invited to join the famous Department of Plant Nutri- tion at the University of California, Berkeley, and there began his career as a plant biochemist. From his arrival in Madison in 1948 until his death in 1983 Green and his colleagues engaged in six areas of re- search: fatty acid oxidation; metallo-flavoproteins; fatty acid synthesis; mitochondria, coenzyme Q, and the respiratory chain complexes; mitochondrial anatomy; and electron trans- port and oxidative phosphorylation. These areas represent unique chapters in Green’s work at the Institute for En- zyme Research.

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122 BIOGRAPHICAL MEMOIRS The Institute for Enzyme Research building was not ready when Green arrived in Madison, and he and his growing research team were housed in an old abandoned building on the engineering campus about two blocks from their final destination. This time is remembered among the team members—though with little nostalgia—as the “barn days.” They continued the cyclophorase work with the aim of im- proving the solubility of some of the fractions obtained so that separation of the individual components of the energy- producing enzyme systems (e.g., pyruvate or fatty acid oxi- dation) could be achieved and their properties documented. They tried various tissue sources and fractionation schemes, using changes of pH and salt concentrations in combina- tion with different centrifugation conditions, but progress was slow and insufficient soluble material for further isola- tion work was produced. During his last months at Columbia and the “barn days” at Wisconsin, Green was able to attract a considerable amount of funds from the National Institutes of Health and particu- larly from the Rockefeller Foundation. The post-World War II period, under the spell of Vannevar Bush’s famous motto “Science, the Endless Frontier,” was a time of generous fi- nancial support for scientific research. It was also a time when federal agencies themselves were seeking worthwhile projects to support. No doubt Green’s skill as a persuasive writer and his flair for picturing the broader implications of his experiments served him well. He was able to equip his laboratory in the new Institute for Enzyme Research building in a grand way, which was unique for those days, and support 10 postdoctoral fellows. Green’s reputation attracted many eager young scien- tists to the Institute for Enzyme Research, including two of us (H.B. and S.J.W.). When the building was first occupied in 1949, there were at least 30 employees, including aca-

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123 DAVID EZRA GREEN demic, technical, and auxiliary staff. Among the first fel- lows who became better known later in their careers were Frank Huennekens, Henry Mahler, Jesse Rabinowitz, Harold Edelhoch, Richard Schweet, Venkataraman Jaganathan, and Rao Sanadi. They were followed by Salih Wakil, Fred Crane, David M. Gibson, Joe Hatefi, Dan Ziegler, Anthony Linnane, Giorgio Lenaz, David Wharton, Gerald Brierley, Alan Se- nior, Alex Tzagoloff, David McLennan, Robert Goldberger, and Roderick Capaldi. These senior fellows would eventu- ally leave the Institute for Enzyme Research for academic appointments at other institutions. Green also provided a temporary haven to several se- nior scientists who had for different reasons an interrup- tion in their careers. Among these were Tom Singer, Edna Kearney, and John Gergely. Often there were other visiting senior scientists in the laboratory. Some visited briefly, oth- ers completed a sabbatical. Among these were Osamu Hayaishi from Japan, Vernon Cheldelin from Oregon State, Walter Nelson from Cornell, Elizabeth Steyn-Parvé from Utrecht, and even Robert Alberty from the Chemistry De- partment at the University of Wisconsin in Madison. The continual presence of such scientists and the ideas and ex- pertise they brought to the Institute for Enzyme Research made it an interesting and stimulating place to be. Green once said during those days, “If we can lick fatty acid oxidation, I will be the happiest of men.” This meant that those who worked most closely with him were involved in this project. Despite their concerted efforts none of the enzyme preparations they produced had sufficient activity to be further purified. The solution to this impasse would come from Henry Lardy and his group, who had moved from the biochemistry department to the second floor of the Institute for Enzyme Research building. One of his stu- dents, George Drysdale, was investigating fatty acid oxida-

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136 BIOGRAPHICAL MEMOIRS resent the first experimental observation and description of the permeability transition that is fundamental for the process of apoptosis, a topic at the forefront of biomedical science today. The observations of the different conformational states of mitochondria led Green to conceive that the process of energy conservation and transfer might be coupled to such conformational transitions. Green realized that ordered and useful conclusions could be arrived at from the large amount of experimental material only by developing suitable theo- retical concepts. Consequently in the late 1960s and through- out the 1970s he preferred to have some postdoctoral fel- lows in his group who were skilled in theoretical chemistry and mathematics; several publications resulted from these collaborations. Although Green’s ideas of an all-embracing theory of electronic transport and energy conservation had elements that are expected to be part of any sound theory of these processes, they were too simplistic and too rigid to have influenced developments in this field. Drawing such a conclusion about Green’s ideas today are unfair, especially when we have the benefit of all the knowledge amassed during the last 30 years to 40 years. The scientific record now includes a large number of high- resolution protein structures that show the actual electron carriers and proton channels in mitochondria, well-founded and experimentally supported theories of electron transfer through peptide chains, and knowledge of electron and hydrogen tunneling. Nevertheless Green did not subscribe to a 1970s theory that has stood the test of time: Peter Mitchell’s chemiosmotic theory. For that reason his name does not appear among the signatories—Paul Boyer, Britton Chance, Lars Ernster, Peter Mitchell, Efraim Racker, and Bill (E. C.) Slater—of the now famous reconciliation and

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137 DAVID EZRA GREEN acceptance statements that were published in volume 46 of the Annual Reviews of Biochemistry in 1977. David Green was a complex person who had an extraordi- nary personality. His life was dedicated fully to research in the field of enzymology. His career in enzymology began in the 1930s when he traveled to Cambridge University in En- gland to pursue a Ph.D. degree in biochemistry. By 1940, at the age of 30, he had written and published his classic work, “The Mechanisms of Biological Oxidations.” Shortly thereafter, at the age of 31, he wrote a classic chapter that was published in volume 1 of the new treatise titled Ad- vances in Enzymology, in which he projected his ideas about the role of vitamins and other trace substances as partici- pants of enzyme function. By the middle of the twentieth century Green was the leading experimentalist in the field of enzymology. He had made significant enough contribu- tions to merit the first Paul-Lewis Award in Enzyme Chem- istry in 1946. Green began his research career isolating and charac- terizing single enzymes. But when he was confronted with the complexities of the intact cell, he directed his energy to detailed studies of organized enzyme systems. As his fame spread throughout the United States immediately after World War II he attracted many junior collaborators both at Co- lumbia University and later at the Institute for Enzyme Re- search. He took an active interest in his junior colleagues, not only by encouraging and inspiring them but also by allowing them to develop their own independent careers. Remarkably and unlike many of his senior colleagues in biochemistry he never insisted on placing his name as co- author on many papers written by his junior colleagues, even when these papers described major discoveries. He established this policy while at Columbia and continued it throughout his career.

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138 BIOGRAPHICAL MEMOIRS Green’s enthusiasm for research was infectious to those who worked side-by-side with him, particularly at Columbia University. When he moved to Wisconsin to set up the Insti- tute for Enzyme Research, he became burdened with the many problems of organizing and operating the institute, finding and hiring talented colleagues, and the ever present problem of procuring funding for his many research activi- ties. Nevertheless Green continued to exhibit the same en- thusiasm for the research conducted by his colleagues. Green’s wife, Doris, was an excellent companion for him and played a very supportive role throughout his career. The Greens had two daughters. Rowena, their elder daugh- ter, was inspired by her father’s enthusiasm for biochemis- try. She is now a distinguished biochemist at the University of Michigan and was elected to the National Academy of Sciences in 2002. Their younger daughter, Pamela, did not choose an academic career. She married and had a daugh- ter, Tammy Baldwin, who currently is a congresswoman rep- resenting the Madison, Wisconsin, district. In recognition of his many contributions to the field of biochemistry the National Academy of Sciences elected Green to membership in 1962. In 1977 a symposium was held in New Orleans to honor Green’s sixty-seventh birthday. His former colleagues Sidney Fleischer, Joe Hatefi, David McLennan, and Alex Tzagoloff organized the symposium under the theme “The Molecular Biology of Membranes,” and many other former colleagues were present to give honor to Green as the scholar and the innovative scientist that he was. A book of the same title is available from Plenum Press, New York and London, 1978, eds. S. Fleischer, Youssef Hatefi, David H. MacLennan, and Alexander Tzagoloff, in which Green presents a summary of his life’s work, and there are anecdotes from many of his collaborators that illustrate the relationship of Green and his disciples. There also was a

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139 DAVID EZRA GREEN celebration of his seventieth birthday that was held in Madi- son. Green became ill during the last years of his life, and his illness and the chemotherapy with which it was treated took a heavy toll on him. Nevertheless he bore his illness with great composure and bravery and never spoke of it. Green succumbed to his illness on July 8, 1983, shortly be- fore his seventy-third birthday, and so ended a life full of great aspirations and accomplishments. According to his wishes there was only a modest memorial service with fam- ily and friends, at which Helmut Beinert gave a eulogy. An obituary by two of us (H.B. and P.K.S.) was published in Trends in Biochemical Sciences in 1983; another by Frank Huennekens was published in Bioenergetics in 1984. WE WISH TO THANK Professor Rowena Matthews, Green’s eldest daughter, and his granddaughter, Congresswoman Tammy Baldwin, for their valuable input into the writing of this biographical memoir, and Professor Frank Huennekens and Youssef Hatefi for the background information on the Institute for Enzyme Research. We especially thank H. F. F. Dixon in the Department of Biochemistry at Cam- bridge University for his very helpful assistance in providing mate- rial from Green’s years at Cambridge. Finally, we thank Jolita Young in the Office of the Home Secretary at the National Academy of Sciences for making available archival biographical material written by Green at the time of his election into the Academy in 1962. AWARDS 1946 Paul-Lewis Award in Enzyme Chemistry (first recipient) 1960 American Academy of Arts and Sciences 1962 National Academy of Sciences

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140 BIOGRAPHICAL MEMOIRS SELECTED BIBLIOGRAPHY David E. Green was a prolific scientist. During his pre- Cambridge and Cambridge days (1931-41) he published, alone or with colleagues, an amazing 36 peer-reviewed pa- pers. During his Harvard stay of one year he and his col- leagues published 3 papers, and during his Columbia stay (1942-49), he and his group published 24 papers. With his move to Wisconsin, over a period of 33 years, 559 scientific publications, including books and review articles, were is- sued. He was the author, coauthor, or editor of 8 books. Listed below is a partial list of notable publications. 1933 The reduction potentials of cysteine, glutathione and glycylcysteine. Biochem. J. 27:678-89. 1937 Reconstruction of the chemical events in living cells. In Perspectives in Biochemistry: Thirty-One Essays Presented to Sir Frederick Gowland Hopkins by Past and Present Members of his Laboratory, eds. J. Needham and D. E. Green, pp. 175-86. Cambridge, U.K.: Cambridge Uni- versity Press. 1940 The Mechanisms of Biological Oxidations, pp 1-178. Cambridge, U.K.: Cambridge University Press. 1941 Enzymes and trace substances. In Advances in Enzymology, vol. 1, eds. F. F. Nord and C. H. Werkman, pp. 177-98. New York: Interscience Publishers. 1953 With H. Beinert, R. W. Von Korff, D. A. Buyske, R. E. Hendschumacher, H. Higgins, and F. M. Strong. A method for the purification of coenzyme A from yeast. J. Biol. Chem. 200:385-400. With H. Beinert, P. Hele, H. Hift, R. W. Von Korff, and C. V.

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141 DAVID EZRA GREEN Ramakrishnan. The acetate activating enzyme system of heart muscle. J. Biol. Chem. 203:35-45. With H. Beinert. Xanthine oxidase, a molybdo-flavoprotein. Biochim. Biophys. Acta 11:599-600. 1954 With S. Mii, H. R. Mahler, and R. M. Bock. Studies on fatty acid oxidizing system of animal tissues. III. Butyryl coenzyme a dehy- drogenase. J. Biol. Chem. 206:1-12. With S. Mii. Studies on the fatty acid oxidizing system of animal tissues. VIII. Reconstruction of fatty acid oxidizing system with triphenyltetrazolium as electron acceptor. Biochim. Biophys. Acta 13:425-32. With S. J. Wakil, S. Mii, and H. R. Mahler. Studies on the fatty acid oxidizing system of animal tissues. VI. Beta-hydroxyacyl coenzyme A dehydrogenase. J. Biol. Chem. 207:631. With B. Mackler and H. R. Mahler. Studies on metallo-flavopro- teins. I. Xanthine oxidase, a molybdoflavoprotein. J. Biol. Chem. 210:149-64. Fatty acid oxidation in soluble systems of animal tissues. Biol. Rev. 29:330-66. 1956 With F. L. Crane, S. Mii, J. G. Hauge, and H. Beinert. On the mechanism of dehydrogenation of fatty acyl derivatives of coen- zyme A. I. The general fatty acyl coenzyme A dehydrogenase. J. Biol. Chem. 218:701. As already indicated in the text of this memoir Green did not list his name as coauthor when he did not directly participate in a research project although his input was critical to the success of the project. Green played an important role in the development of the specific research project in the following important papers. 1953 H. Beinert, R. M. Bock, D. S. Goldman, H. R. Mahler, S. Mii, P. G. Stansly, and S. J. Wakil. The reconstruction of the fatty acid oxi- dizing system of animal tissues. J. Am. Chem. Soc. 75:4111-12. H. R. Mahler, S. J. Wakil, and R. M. Bock. Studies on fatty acid

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142 BIOGRAPHICAL MEMOIRS oxidation. I. Enzymatic activation of fatty acids. J. Biol. Chem. 204:453-68. H. R. Mahler and D. G. Elowe. DPNH-Cytochrome reductase, a ferro-flavoprotein. J. Am. Chem. Soc. 75:5769. 1954 S. J. Wakil and H. R. Mahler. Studies on the fatty acid oxidizing system of animal tissues. V. Unsaturated fatty acyl coenzyme A hydrase. J. Biochem. Chem. 207:125. D. S. Goldman. Studies on the fatty acid oxidizing system of animal tissues. VII. The beta-ketoacyl coenzyme A cleavage enzyme. J. Biol. Chem. 208:345. 1956 F. L. Crane and H. Beinert. On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. II. The electron-transfer- ring flavoprotein. J. Biol. Chem. 218:717. J. G. Hauge, F. L. Crane, and H. Beinert. On the mechanism of dehydrogenation of fatty acid derivatives of coenzyme A. III. Palmityl CoA dehydrogenase. J. Biol. Chem. 219:727. 1957 D. M. Gibson, M. I. Jacob, J. W. Porter, A. Tietz, and S. Wakil. Biosynthesis of fatty acids by soluble enzyme fractions. Biochim. Biophys. Acta 23:219. F. L. Crane and J. L. Glenn. Studies on the terminal electron trans- port system. VI. Fragmentation of the electron transport particle with Deoxycholate. Biochim. Biophys. Acta 24:100. S. J. Wakil, J. W. Porter, and D. M. Gibson. Studies on the mecha- nism of fatty acid synthesis. I. Preparation and purification of an enzyme system for reconstruction of fatty acid synthesis. Biochim. Biophys. Acta 24:453. F. L. Crane, Y. Hatefi, R. L. Lester, and C. Widmer. Isolation of a quinone from beef heart mitochondria. Biochim. Biophys. Acta 25:220. J. W. Porter, S. J. Wakil, A. Tietz, M. I. Jacob, and D. M. Gibson. Studies on the mechanism of fatty acid synthesis. II. Cofactor requirements of the soluble pigeon liver system. Biochim. Biophys. Acta 25:35.

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143 DAVID EZRA GREEN 1958 D. M. Gibson, E. B. Titchener, and S. J. Wakil. Requirement for bicarbonate in fatty acid synthesis. J. Am. Chem. Soc. 80:2908. S. J. Wakil, E. B. Titchener, and D. M. Gibson. Evidence for the participation of biotin in the enzymic synthesis of fatty acids. Biochim. Biophys. Acta 29:225. R. L. Lester, F. L. Crane, and Y. Hatefi. Coenzyme Q: A new group of quinones. J. Am. Chem. Soc. 80:4751. D. M. Gibson, E. B. Titchener, and S. J. Wakil. Studies on the mechanism of fatty acid synthesis V. Bicarbonate requirement for the synthe- sis of long-chain fatty acids. Biochim. Biophys. Acta 30:376. S. J. Wakil. A malonic acid derivative as an intermediate in fatty acid synthesis. J. Am. Chem. Soc. 80:6465. 1959 R. L. Lester and S. Fleischer. The specific restoration of succinoxi- dase activity by coenzyme Q compounds in acetone-extracted mi- tochondria. Biochim. Biophys. 80:470. F. L. Crane, C. Widmer, R. L. Lester, and Y. Hatefi. Studies on the electron transport system. XV. Coenzyme Q (Q275) and the suc- cinoxidase activity of the electron transport particle. Biochim. Biophys. Acta 3l:476. Y. Hatefi, R. L. Lester, F. L. Crane, and C. Widmer. Studies on the electron transport system. XVI. Enzymic oxidoreduction reactions of coenzyme Q. Biochim. Biophys. Acta 3l:490. F. L. Crane, R. L. Lester, C. Widmer, and Y. Hatefi. Studies on the electron transport system. XVIII. Isolation of coenzyme Q (Q274) from beef heart and beef heart mitochondria. Biochim. Biophys. Acta 32:73. R. L. Lester, Y. Hatefi, C. Widmer, and F. L. Crane. Studies on the electron transport system. XX. Chemical and physical properties of the coenzyme Q family of compounds. Biochim. Biophys. Acta 33:169. R. L. Lester and F. L. Crane. The natural occurrence of coenzyme Q and related compounds. J. Biol. Chem. 234:2169. S. J. Wakil, E. B. Titchener, and D. M. Gibson. Studies on the mechanism of fatty acid synthesis. VI. Spectrophotometric assay and stoichi- ometry of fatty acid synthesis. Biochim. Biophys. Acta 34:227.

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144 BIOGRAPHICAL MEMOIRS D. M. Ziegler and K. A. Doeg. The isolation of a functionally intact succinic dehydrogenase-cytochrome B complex from beef heart mitochondria. Arch. Biochem. Biophys. 85:282. 1960 J. Ganguly. Studies on the mechanism of fatty acid synthesis. VII. Biosynthesis of fatty acids from malonyl CoA. Biochim. Biophys. Acta 40:110. S. J. Wakil and D. M. Gibson. Studies on the mechanism of fatty acid synthesis. VIII. The participation of protein-bound biotin in the biosynthesis of fatty acids. Biochim. Biophys. Acta 41:122. H. Beinert and R. H. Sands. Studies on succinic and DPNH dehy- drogenase preparations by paramagnetic resonance (EPR) spec- troscopy. Biochem. Biophys. Res. Commun. 3:41. R. H. Sands and H. Beinert. Studies on Mitochondria and submito- chondrial particles by paramagnetic resonance (EPR) spectros- copy. Biochem. Biophys. Res. Commun. 3:47. K. S. Ambe and F. L. Crane. Studies on the electron transport sys- tem XXVI. Specificity of coenzyme Q and coenzyme Q deriva- tives. Biochim. Biophys. Acta 43:30. 1961 D. E. Griffiths and D. C. Wharton. Copper in cytochrome oxidase. Biochem. Biophys. Res. Commun. 4:199. Y. Hatefi, A. G. Haavik, and D. E. Griffiths. Reconstitution of the electron transport system. I. Preparation and properties of the interacting enzyme complexes. Biochem. Biophys. Res. Commun. 4:441. H. Beinert and W. Lee. Evidence for a new type of iron containing electron carrier in mitochondria. Biochem. Biophys. Res. Commun. 5:40. L. R. Fowler and Y. Hatefi. Reconstitution of the electron transport system III. Reconstitution of DPNH oxidase, succinic oxidase, and DPNH, succinic oxidase. Biochem. Biophys. Res. Commun. 5:203. D. E. Griffiths and D. C. Wharton. Studies of the electron transport system. XXXV. Purification and properties of cytochrome oxi- dase. J. Biol. Chem. 236:1850.

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