Harland Goff Wood, September 2, 1907—September 12, 1991 | By David A. Goldthwait and Richard W. Hanson | Biographical Memoirs
BIOGRAPHICAL MEMOIRS National Academy of Sciences

Harland Goff Wood, photo

Harland Goff Wood, signature
Harland Goff Wood
September 2, 1907 — September 12, 1991
By David A. Goldthwait and Richard W. Hanson

HARLAND GOFF WOOD, who was descended from William Goffe (b. 1619), one of the appointed judges responsible for the beheading of King Charles I, was born on September 2, 1907, in the small town of Delavan, Minnesota. His parents, both of whom had only a high school education, taught their four sons and one daughter to work hard and to be self-reliant--the result for the sons: two Ph.D.s, one Ph.D.-M.D., one M.D., and one LL.B; and for the daughter: an honorary LL.D. It is hard to picture Harland Wood as a frail child who spent two years in kindergarten and two years in the first grade. He and his brothers helped on the family's farm in Mankato, Minnesota, walking the mile home from school at noon to water the stock and then running back after lunch. At Macalester College in Minnesota, he majored in chemistry and there met Mildred Davis, whom he married in 1929. In 1931 he was accepted as a graduate student in bacteriology at Iowa State University at Ames by C. H. Werkman, who was starting to investigate the chemistry of bacterial fermentations. It was there that Harland made his stunning discovery of CO2 fixation, which up to that time was known to occur only in chemosynthetic and photosynthetic autotrophs. This idea was so controversial that for some time Professor Werkman doubted the validity of Harland's findings.

From 1935 to 1936 Harland worked as a fellow with W. H. Petersen at the University of Wisconsin, and it was here that he joined Ed Tatum in studying the growth factor requirements for propionibacteria. Harland returned to Werkman's department in 1936 to focus on CO2 fixation, as will be discussed. Although Harland was tremendously productive at Ames, building a thermal diffusion column for the isolation of 13C as well as a mass spectrometer to measure the isotope, Werkman would not initially allow him to work on animals and would not arrange for Harland's future independence at Ames. And so in 1943 he moved to the Department of Physiological Chemistry at the University of Minnesota, and it was there that he used 13C-NaHCO3 labeling of the different carbon atoms of the glucose of rat liver glycogen to study the pathways of glucose synthesis.

In 1946 Harland accepted the position of chairman of the Department of Biochemistry at the School of Medicine of what was then Western Reserve University in Cleveland, Ohio, on the condition, as he told Dean Joseph Wearn, that he be allowed to go deer hunting with his father and four brothers each autumn. He loved duck and deer hunting and even at seventy-nine years of age was seen 35 feet up a tree waiting for a deer. As chairman he brought in an entirely new faculty that was oriented to the use of isotopic tracers to study a variety of metabolic pathways. Under Harland's direction, this young and energetic group, which included future members of the National Academy of Sciences, Merton Utter and Lester Krampitz, created an outstanding national reputation for the department. At the local level, he was also unique. Harland instituted a policy that all honoraria, even for participating in study sections, should go into a student travel fund, since he felt that outside activities should have an intrinsic value based on science and not on money--echoes of William Goffe. Departmental seminars were at noon on Saturday and monthly staff meetings were held after that, often until 5:00 p.m., when they were terminated by telephone calls from irate wives. There was a pooling of resources, a sharing of all equipment, and a camaraderie that would be difficult to equal in these times.

Harland Wood spent the last forty-five years of his career at Case Western Reserve University (Western Reserve University merged with Case Institute of Technology in 1968). He retired as chairman in 1965 so that he could have more time for research, and for Harland this meant research at the bench, not just at the desk. He continued "pounding the bench," as he called it, right up until a few days before his death on September 12, 1991. Lymphoma was diagnosed four years before his death; he died of a fall that resulted in a ruptured spleen. Harland had undergone chemotherapeutic cycles several times, but they never significantly halted his scientific activities. At the time of his death, he held three grants from the National Institutes of Health, had a working group of fifteen associates, and was writing nine manuscripts. At the last meeting of the ASBMB that he attended, he had twelve posters on display and was present to discuss results related to each of them. Between his seventieth birthday and his death, he published ninety-six papers, all in well-respected journals--surely a record for an "elderly" biochemist. He is survived by his wife Mildred and two daughters.

Harland Wood left a long and distinguished record in the life sciences, beginning with his pioneering work with C. H. Werkman at Iowa State College, which demonstrated for the first time that CO2 is utilized in heterotrophic organisms. In 1935 he demonstrated that the prevailing dogma that CO2 was utilized only by bacterial autotrophs was incorrect. In a series of studies he determined the products formed from the fermentation of glycerol by propionic acid bacteria in a bicarbonate buffer system and calculated the carbon and oxidation-reduction balances to account for the carbon of the fermented substrate and to ensure that there was a balance of the oxidation-reduction state of substrates and products. Surprisingly, more carbon was found in the products than was supplied by the fermented glycerol. He subsequently discovered that the extra carbon was derived from CO2 in the buffer and that oxidation balanced reduction when the reduction of CO2 was taken into account. He proposed that CO2 and pyruvate combined to form oxa-lacetate, which subsequently was reduced to succinate. This pyruvate-CO2 reaction became known as the Wood-Werkman reaction.

When isotopic tracers of carbon became available in the late 1930s, Harland was among the first to exploit isotopes in biological studies. He was a true pioneer in developing procedures for the use of these isotopes for metabolic tracer studies. As previously noted, he built a water-cooled thermal diffusion column in a five-story elevator shaft for the separation of 13C isotopic carbon. Harland was always fond of describing the day that he found the column warped and distorted due to a temporary drop in the water pressure. This drop, he finally discovered, occurred when the home economics class let out and three toilets were flushed simultaneously! To measure 13C, he also built a mass spectrometer. His innovative work initially provided evidence that citrate was not part of the citric acid cycle because he had assumed that citrate was a symmetrical molecule. In his characteristic manner, he later said in a Lynen Lecture that even though he was wrong it was one of his "most important contributions" to biochemistry. The studies by Wood and his colleagues in 1945 clearly demonstrated the pathway of CO2 incorporation into specific carbon atoms of glucose derived from hepatic glycogen. Harland graduated briefly from bacteria to cows, where his farm background helped in the injection of 14C glucose into the artery going to the right udder. Subsequently, by personally milking each side, he determined that lactose was synthesized from free glucose rather than glucose-1-phosphate and that it was glucose that reacted with UDP-galactose to form lactose. In collaboration with Joseph Katz and Bernard R. Landau, Harland also developed methods to estimate the proportion of carbohydrate metabolized in the pentose pathway and glycolysis by studying 14C distributions in glucose and glycogen. These latter studies were instrumental in establishing the stoichiometry of the pentose pathway.

The overall direction of Harland's research over sixty years continued to be on CO2 fixation. During the last thirty years of his life, he focused on establishing the reaction mechanism of transcarboxylase (TC) from propionibacteria. This is a key enzyme in the propionic acid cycle, and it transfers a carboxyl group in the conversion of methylmalonyl CoA + pyruvate to propionyl CoA + oxalacetate. The enzyme is also extremely complex, with six identical central subunits, each with two CoA-binding sites, six dimeric outside subunits each of the six with two keto acid sites, and twelve small biotinyl subunits that carry the carboxyl groups between the CoA and keto sites. The kinetics of the reaction did not fit the accepted mechanisms, so Dexter Northrup, then a student with Harland, proposed a new kinetic mechanism for TC that was later verified by Northrup and Wood. Extensive work was done on the separation of the three subunits of TC and on the reconstitution of enzyme activity. Together with a number of associates, Wood studied the quaternary structure of TC by electron microscopy, and this revealed the "Mickey Mouse" enzyme. Using thin crystals of the enzyme, resolution of the structure at 10 Å was possible by microscopy. The primary amino acid sequence of the biotinyl subunit was determined, and, in collaboration with David Samols, the genes for all three subunits were cloned and sequenced. At the end of his life, Harland was studying the enzymatic properties of a large number of mutants that were generated in the three different subunits and was doing many of the enzyme assays himself. These studies were of great interest because of the complexity of the subunit structure of the enzyme and the ability to examine different aspects of function.

Harland Wood also discovered a novel pathway for carbon monoxide (CO) fixation in acetogens, a group of anaerobic bacteria that synthesize acetate from CO or CO2/H2. This new pathway of autotrophic growth, demonstrated in Clostridium thermoaceticum and Acetobacterium woodii, differs from all previously described pathways for autotrophic growth, such as the Calvin reductive pentose cycle or the tricarboxylic acid cycle. Much of Harland's work in the area was done in collaboration with Lars Ljundahl, both at Case Western Reserve University and the University of Georgia. The mechanism of this pathway involves reduction of CO2 to methyltetrahydrofolate and transfer of the methyl group to a corrinoid protein. The methyl group is then transferred to carbon monoxide dehydrogenase (CODH); CO and CoASH/moieties combine with CODH, which catalyzes the formation of acetyl-CoA from the above three groups. Thus, CODH plays a central role in this pathway. Most of the enzymes involved in the various steps of the pathway were purified to homogeneity. The availability of purified enzymes permitted Harland and his collaborators to dissect the pathway and define the role of each enzyme. Detailed studies toward elucidating the mechanism of action of CODH were initiated. CODH contains six nickel, three zinc, thirty-two iron atoms, forty-two labile sulfides and has three acceptor sites: one for the methyl group transferred from the methyl corrinoid enzyme, a CO site, and a CoASH site. From ESR studies it was shown that the Ni-Fe center is involved in the interaction of the CO group with CODH. Also, the methyl group is bound to a cysteine residue of CODH. The CoASH substrate site has been characterized using fluorescence spectroscopy, circular dichroism, and chemical modification. From these studies it was proposed that both tryptophan(s) and arginine(s) are involved in the binding of CoASH to CODH. Even from this brief review it is clear that Harland Wood, over the sixty years that he was involved in research, "followed the trail of CO2."

Harland Wood was also a pioneer in studying the role of pyrophosphate and polyphosphate as energy sources. It has long been accepted that the energy contained in the anhydride bond of pyrophosphate is not utilized efficiently by cells. However, Harland, together with Nelson Phillips, showed this not to be true by the isolation and characterization of bacterial enzymes that utilize pyrophosphate in reaction with oxaloacetate, with phosphoenolpyruvate, and with fructose-6-phosphate. Inorganic polyphosphates have been considered by others as primitive sources of energy. Harland extensively studied the enzymatic synthesis of polyphosphate from ATP and showed that a bacterial glucokinase utilizes polyphosphate much more effectively than ATP in the reaction with glucose. Two separate sites exist on the enzyme for these two sources of high-energy phosphate. This enzyme may represent an intermediate stage of evolution from a polyphosphate-dependent metabolism to an ATP-dependent metabolism.

Harland Wood's outstanding career was marked by many innovations. However, what most characterized Harland was his scientific style. He was remarkable for several reasons. First, one could always feel the sense of excitement and drive that he brought to the experimental aspect of science. The focus of the excitement was always on discovery. Second, he continually developed and applied the latest technology to his experimental problem. There were many jumps from fermentation balances all the way to gene sequencing. Finally, he was able to collaborate with others very productively, particularly those with expertise in specific areas where the scientific results could not have been achieved by either group alone. The flavor of the man and his approach to science are best captured by Harland himself in his autobiography in the Annual Review of Biochemistry in 1985.

Harland Wood's outstanding career was marked by many innovations in other areas. As chairman of the biochemistry department at Western Reserve University, he led the curriculum reform that resulted in an integrated organ-system-based method for teaching the first two years of medical school; this curriculum has had a great impact on medical education nationally. He swayed the faculty to vote for the new curriculum with the challenge, "How do you guys know it's not going to work unless you run the experiment?" He served as chairman of the biochemistry department for twenty years, as dean of sciences at Case Western Reserve University from 1967 to 1969, and finally as university professor and university professor emeritus from 1970 to 1991.

Harland Wood was president of the American Society of Biological Chemistry from 1959 to 1960. First as secretary-general and then as president of the International Union of Biochemistry in 1982-83, he did a great deal for that organization's revitalization. He served on many study sections, and his strong support for younger biochemists during his tenure on one of those study sections became known as "The Wood Factor." He was a member of many advisory boards and served as an editorial board member of a number of important journals. As a young member of the Editorial Board of the Journal of Biological Chemistry, he was instrumental in eliminating self-perpetuating appointments when he resigned after five years and argued, "Listen, if all you guys died tomorrow, a good board could be picked the next day to replace you." He received a number of prestigious awards, including the Eli Lilly Award, the Carl Neuberg Medal, the Lynen Lecture Medal, the Waksman Award, the Rosenstiel Award, the Michaelson-Morly Award, and the National Medal of Science. He held honorary degrees from Macalester College, Northwestern University, the University of Cincinnati, and Case Western Reserve University. He was a member of the National Academy of Sciences, the American Academy of Arts and Sciences, and the Biochemical Society of Japan and served on the President's Science Advisory Committee under Presidents Johnson and Nixon.

In a 1985 Annual Review of Biochemistry article, Harland Wood wrote that "scientists are the fortunate few who earn a livelihood by pursuit of a hobby. This hobby sometimes consumes their every thought, but usually it provides a deeply satisfying life." He continued, "Many highly successful scientists desert the laboratory bench early in their careers and thereafter direct the research of their co-workers. My goal has been to remain personally active in the laboratory as long as I am involved in science." And so he did.

Over the sixty years that Harland Wood spent in science, he made countless friends in many countries who revered him not just for his accomplishments but for his intellectual honesty. Here was a man without pretensions, whose opinions and decisions were always based on principles and not on personal factors, a man whose mind was open to new ideas and concepts, a man who by his example and encouragement got the best out of his associates, and a man who, once he made up his mind, would drive straight toward his goal. In him one felt the warmth, strength, and integrity that made him unique and irreplaceable.

SELECTED BIBLIOGRAPHY

1933
With O. L. Osburn and C. H. Werkman. Determination of formic, acetic and propionic acids in a mixture. Ind. Eng. Chem. Analyt. Ed. 5:247-50.
1934
With C. H. Werkman. The propionic acid bacteria: On the mechanism of glucose dissimilation. J. Biol. Chem. 105:63-72.
With C. H. Werkman. Pyruvic acid in the dissimilation of glucose by the propionic acid bacteria. Biochem. J. 28:745-47.
With C. H. Werkman. Intermediate products of the propionic acid fermentation. Proc. Soc. Exp. Biol. Med. 31:938-40.
With C. H. Werkman. The utilization of agricultural by-products in the production of propionic acid by fermentation. J. Agric. Res. 49:1017-20.
1935
With C. H. Werkman. The utilization of CO2 by the propionic acid bacterial in the dissimilation of glycerol. J. Bacteriol. 30:332 (Abstract).
With C. H. Werkman. The isolation and possible intermediary role of formaldehyde in the propionic acid fermentation. J. Bacteriol. 30:652-53.
1936
With C. H. Werkman. The utilization of CO2 in the dissimilation of glycerol by the propionic acid bacteria. Biochem. J. 30:48-53.
With C. H. Werkman. Mechanism of glucose dissimilation by the propionic acid bacteria. Biochem. J. 30:618-23.
With R. W. Stone and C. H. Werkman. Activation of the lower fatty acids by propionic acid bacteria. Biochem. J. 30:624-28.
With C. Erb and C. H. Werkman. A macro-respirometer for the study of aerobic bacterial dissimilation. Iowa State Coll. J. Sci. 10:295-302.
With C. Erb and C. H. Werkman. The aerobic dissimilation of lactic acid by the propionic acid bacteria. J. Bacteriol. 31:595-602.
With O. L. Osburn and C. H. Werkman. Determination of volatile fatty acids by the partition method. Ind. Eng. Chem. Analyt. Ed. 8:270-75.
With E. L. Tatum and W. H. Peterson. Growth factors for bacteria. V. Vitamin B12: a growth stimulant for propionic acid bacteria. Biochem. J. 30:1898-1904.
With E. L. Tatum and W. H. Peterson. Essential growth factors for the propionic acid bacteria. II. Nature of the Neuberg precipitate fraction of potato. J. Bacteriol. 32:167-74.
1937
With A. A. Anderson and C. H. Werkman. Growth factors for the propionic and lactic acid bacteria. Proc. Soc. Exp. Biol. Med. 36:217-19.
With C. Erb and C. H. Werkman. Dissimilation of pyruvic acid by the propionic acid bacteria. Iowa State Coll. J. Sci. 11:287-92.
With R. W. Stone and C. H. Werkman. The intermediate metabolism of the propionic acid bacteria. Biochem. J. 31:349-59.
With E. L. Tatum and W. Peterson. Growth factors for bacteria. IV. An acidic ether soluble factor essential for growth of propionic acid bacteria. J. Bacteriol. 33:227-42.
With C. H. Werkman and R. W. Stone. The dissimilation of phosphate esters by the propionic acid bacteria. Enzymologia 4:24-30.
1938
With A. A. Anderson and C. H. Werkman. Nutrition of the propionic acid bacteria. J. Bacteriol. 36:201-13.
With C. H. Werkman. The utilization of CO2 by the propionic acid bacteria. Biochem. J. 32:1262-71.
With W. P. Wiggert and C. H. Werkman. The fermentation of phosphate esters by the propionic acid bacteria. Enzymologia 2:373-76.
1939
With R. W. Brown and C. H. Werkman. Nutrient requirements of butyric acid butyl alcohol bacteria. J. Bacteriol. 38:631-40.
1940
With C. R. Brewer, M. N. Mickelson, and C. H. Werkman. A macrorespirometer for the study of the aerobic metabolism of microorganism. Enzymologia 8:314-17.
With C. Geiger and C. H. Werkman. Nutritive requirements of the heterofermentative lactic acid bacteria. Iowa State Coll. J. Sci. 14:367-78.
With C. H. Werkman. The fixation of CO2 by cell suspensions of Propionibacterium pentesaceum. Biochem. J. 34:7-14.
With C. H. Werkman. The relationship of bacterial utilization of CO2 to succinic acid formation. Biochem. J. 34:129-38.
With C. H. Werkman. Gewinnung-Freigelester Enzyme Specialmethoden fur Bakterien Die Methoden der Fermentforschung, ed. Oppenheimer. Leipzig: George Thiem.
With C. H. Werkman, A. Hemingway, and A. O. Nier. Heavy carbon as a tracer in bacterial fixation of CO2. J. Biol. Chem. 135:789-90.
1941
With H. D. Slade, A. O. Nier, A. Hemingway, and C. H. Werkman. Note on the utilization of carbon dioxide by heterotrophic bacteria. Iowa State Coll. J. Sci. 15:339-41.
With C. H. Werkman, A. Hemingway, and A. O. Nier. Position of carbon dioxide-carbon in propionic acid synthesized by Propionibacterium. Proc. Soc. Exp. Biol. Med. 46:313-16.
With C. H. Werkman, A. Hemingway, and A. O. Nier. Note on the degradation of propionic acid synthesized by Propionibacterium. Iowa State Coll. J. Sci. 15:213-14.
With C. H. Werkman, A. Hemingway, and A. O. Nier. Mechanism of fixation of carbon dioxide in the Krebs cycle. J. Biol. Chem. 139:483-84.
With C. H. Werkman, A. Hemingway, and A. O. Nier. Heavy carbon as a tracer in heterotrophic carbon dioxide assimilation. J. Biol. Chem. 139:365-76.
With C. H. Werkman, A. Hemingway, and A. O. Nier. Heavy carbon dioxide in succinic acid synthesized by heterotrophic bacteria. J. Biol. Chem. 139:377-81.
With C. H. Werkman, A. Hemingway, A. O. Nier, and C. G. Stuckwisch. Reliability of reactions used to locate assimilated carbon in propionic acid. J. Am. Chem. Soc. 2140-42.
1942
Criteria for experiments with isotopes. In Symposium on the Respiratory Enzymes and the Biological Action of Vitamins, ed. E. A. Evans, Jr., pp. 252-56. Chicago: University of Chicago Press.
With H. D. Slade, A. O. Nier, A. Hemingway, and C. H. Werkman. Assimilation of heavy carbon dioxide by heterotrophic bacteria. J. Biol. Chem. 143:133-45.
With C. H. Werkman. On the metabolism of bacteria. Bot. Rev. 8:1-68.
With C. H. Werkman. Heterotrophic assimilation of carbon dioxide. Adv. Enzymol. 2:135-82.
With C. H. Werkman, A. Hemingway, and A. O. Nier. Fixation of carbon dioxide by pigeon liver in the dissimilation of pyruvic acid. J. Biol. Chem. 142:31-45.
1943
With G. Kalnitsky and C. H. Werkman. CO2-fixation and succinic acid formation by a cell-free enzyme preparation of Escherichia coli. Arch. Biochem. 2:269-81.
With L. O. Krampitz and C. H. Werkman. Enzymatic fixation of carbon dioxide in oxalacetate. J. Biol. Chem. 147:243-53.
1944
Metabolism of nervous tissue in poliomyelitis. Lancet 64:240-42.
With R. W. Brown and C. H. Werkman. Fixation of carbon dioxide in lactic acid by Clostridium butylicum. Arch. Biochem. 5:423-33.
With R. W. Brown, C. H. Werkman, and C. G. Stuckwisch. The degradation of heavy-carbon butyric acid from butyl alcohol fermentation. J. Am. Chem. Soc. 66:1812-18.
With I. I. Rusoff and J. M. Reiner. Anaerobic glycolysis of the brain in experimental poliomyelitis. J. Exp. Med. 81:151-59.
1945
With R. W. Brown and C. H. Werkman. Mechanism of the butyl alcohol fermentation with heavy carbon acetic and butyric acids and acetone. Arch. Biochem. 6:243-60.
With N. Lifson and V. Lorber. The position of fixed carbon in glucose from rat liver. J. Biol. Chem. 159:475-89.
With V. Lorber and N. Lifson. Incorporation of acetate carbon into rat liver glycogen by pathways other than carbon dioxide fixation. J. Biol. Chem. 161:411-12.
With I. I. Rusoff. The protective action of trypan red against infection by a neurotropic virus. J. Exp. Med. 82:297-309.
With M. F. Utter. Fixation of carbon dioxide in oxalacetate by pigeon liver. J. Biol. Chem. 160:375-76.
With M. F. Utter and J. M. Reiner. Measurement of anaerobic glycolysis of brain as related to poliomyelitis. J. Exp. Med. 82:217-26.
With M. F. Utter and J. M. Reiner. Anaerobic glycolysis in nervous tissue. J. Biol. Chem. 161:197-217.
With B. Vennesland and E. A. Evans. The mechanism of carbon dioxide fixation by cell-free extracts of pigeon liver: distribution of labeled carbon dioxide in the products. J. Biol. Chem. 159:153-58.
1946
The fixation of carbon dioxide and the interrelationships of the tricarboxylic acid cycle. Physiol. Rev. 26:198-246.
With V. Lorber, N. Lifson, and J. Barcroft. The metabolism of acetate by the completely isolated mammalian heart investigated with carboxyl labeled acetate. Am. J. Physiol. 145:557-60.
With M. F. Utter. The fixation of carbon dioxide in oxalacetate by pigeon liver. J. Biol. Chem. 164:455-76.
1948
Tracer studies on the intermediary metabolism of carbohydrates. In Symposium on the Use of Isotopes in Biology and Medicine, pp. 209-42. Madison: University of Wisconsin Press.
The synthesis of liver glycogen in the rat as an indicator of intermediary metabolism. Cold Spring Harbor Symp. Quant. Biol. 13:201-10.
With N. Lifson, V. Lorber, and W. Sakami. The incorporation of acetate and butyrate carbon into rat liver glycogen by pathways other than carbon dioxide fixation. J. Biol. Chem. 176:1263-84.
1949
Tracer studies on the intermediary metabolism of carbohydrates. In Isotopes in Biology and Medicine. Madison: University of Wisconsin Press.
With V. Lorber. Carbohydrate metabolism. Ann. Rev. Biochem. 18:299-334.
With W. Shreeve, V. Fell, and V. Lorber. The distribution of fixed radioactive carbon in glucose from rat liver glycogen. J. Biol. Chem. 177:679-82.
1950
Symposium on chemical transformation of carbons in photosynthesis. Fed. Proc. 9:553-55.
A consideration of some reactions involving CO2 fixation. Symp. Soc. Exp. Biol. 5:9-28.
With V. Lorber, N. Lifson, and W. Sakami. Conversion of propionate to liver glycogen in the intact rat, studied with isotopic propionate. J. Biol. Chem. 183:531-38.
With V. Lorber, N. Lifson, W. Sakami, and W. W. Shreeve. Conversion of lactate to liver glycogen in the intact rat studied with isotopic lactate. J. Biol. Chem. 183:517-29.
With H. J. Strecker and L. O. Krampitz. Fixation of formic acid in pyruvate by a reaction not utilizing acetyl phosphate. J. Biol. Chem. 182:525-40.
1951
A study of acetone metabolism using glycogen and serine as indicators and the roles of C1-compounds in metabolism. In Ciba Foundation Conference on Isotopes in Biochemistry, ed. G. E. W. Wolstenholme, pp. 227-45. London: Churchill.
With M. F. Utter. Mechanisms of fixation of CO2 by heterotrophs and autotrophs. Adv. Enzymol. 12:41-151.
1952
The metabolism of formate by animals. Harvey Lect. Ser. 14:127-48.
A study of CO2-fixation by mass determination of the types of 13C-acetate. J. Biol. Chem. 194:905-31.
Fermentation of 3,4-C14 and 1-C14-labeled glucose by Clostridium thermoaceticum. J. Biol. Chem. 199:579-83.
1953
With F. W. Leaver. CO2 turnover in the fermentation of 3,4,5 and 6 carbon components by the propionic acid bacteria. Biochim. Biophys. Acta 12:207-22.
With F. W. Leaver. Evidence from fermentation of labeled substrates which is inconsistent with present concepts of the propionic acid fermentation. J. Cell. Comp. Physiol. 41:225-40.
1954
With G. Popjak. Biological asymmetry of glycerol and formation of asymmetrically labeled glucose. J. Biol. Chem. 206:875-82.
With P. Schambye. The in vivo conversion of 14C-glycerol into rat liver glycogen. In Radioisotope Conference, vol. 1, pp. 346-50.
1955
Significance of alternate pathways in the metabolism of glucose. Physiol. Rev. 35:841-59.
With I. A. Bernstein, K. Lentz, M. Malm, and P. Schambye. Degradation of glucose C14 with Leuconostoc mesenteroides: alternate pathways and tracer patterns. J. Biol. Chem. 215:137-52.
With R. G. Kulka and N. L. Edson. Fermentation of glucose-1-C14 in cell-free extracts of Propionibacteria. Proc. Univ. Otago 33:24-25.
With F. W. Leaver and R. Stjernholm. The fermentation of three carbon substrates by Clostridium propionicum and Propionibacterium. J. Bacteriol. 70:521-30.
With K. Lentz. Synthesis of acetate from formate and carbon dioxide by Clostridium thermoaceticum. J. Biol. Chem. 215:645-54.
With R. Stjernholm and F. W. Leaver. The metabolism of labeled glucose by the propionic acid bacteria. J. Bacteriol. 70:510-20.
1956
The teaching of biochemistry in an integrated medical curriculum. Fed. Proc. 15:865-70.
With R. G. Kulka and N. L. Edson. The metabolism of 14C-glucose in an enzyme system from Propionibacterium. Biochem. J. 63:177-82.
With R. Stjernholm and F. Leaver. The role of succinate as a precursor of propionate in the propionic acid fermentation. J. Bacteriol. 72:142-52.
1957
Transactions of the Third Conference of Polysaccharides in Biology. New York: Josiah Macy, Jr. Foundation.
With I. A. Bernstein. Determination of isotopic carbon patterns in carbohydrate by bacterial fermentation. Methods Enzymol. 4:561-83.
With H. Gest. Determination of formate. In Methods in Enzymology, vol. 3, ed. S. Colowick and N. Kaplan, pp. 285-92. New York: Academic Press.
With P. Schambye and M. Kleiber. Lactose synthesis. I. The distribution of C14 in lactose of milk after intravenous injection of C14 compounds. J. Biol. Chem. 226:1011-21.
With P. Schambye and G. J. Peeters. Lactose synthesis. II. The distribution of C14 in lactose of milk from perfused isolate cow udder. J. Biol. Chem. 226:1023-34.
With P. M. L. Siu and P. Schambye. Lactose synthesis. III. The distribution of C14 in lactose of milk after intra-arterial injection of acetate-l-C14. Arch. Biochem. Biophys. 69:390-404.
1958
Tracer studies on the synthesis of milk constituents. In Proceedings 2nd International Conference on Peaceful Uses of Atomic Energy, pp. 50-57. New York: Pergamon Press.
With R. Gillespie, S. Joffee, R. G. Hansen, and H. Hardenbrook. Lactose synthesis. V. C14 in lactose, glycerol and serine as indicators of the triose phosphate isomerase reaction and pentose cycle. J. Biol. Chem. 233:1271-78.
With J. Katz. The distribution of C14 in the hexose phosphates and the effect of recycling in the pentose cycle. J. Biol. Chem. 233:1279-82.
With S. H. Pomerantz. A mass analysis study of formaldehyde fixation and cleavage of lactate by Propionibacterium arabinosum. J. Biol. Chem. 231:519-31.
With S. Joffe, R. Gillespie, R. G. Hansen, and H. Hardenbrook. Lactose synthesis. IV. The synthesis of milk constituents after unilateral injection of glycerol-1,3-C14. J. Biol. Chem. 233:1264-70.
With R. L. Stjernholm. Differential degradation of D- and L- glycerol-1-C14 by A. aerogenes. Arch. Biochem. Biophys. 78:28-32.
1959
With R. Gillespie, R. G. Hansen, W. A. Wood, and H. Hardenbrook. Arteriovenous 14CO2 differences and the pentose cycle in the cow's udder. Biochem. J. 73:694-701.
With P. M. L. Siu. Conversion of galactose and glucose to liver glycogen in vivo. J. Biol. Chem. 234:2223-26.
1960
With J. Katz. The use of glucose-C14 for the evaluation of the pathways of glucose metabolism. J. Biol. Chem. 235:2165-77.
With R. L. Stjernholm. Trehalose and fructose as indicators of metabolism of labeled glucose by the propionic acid bacteria. J. Biol. Chem. 235:2753-61.
With R. L. Stjernholm. Glycerol dissimilation and the occurrence of symmetrical three-carbon intermediate in the propionic acid fermentation. J. Biol. Chem. 235:2757-61.
With R. W. Swick. The role of transcarboxylase in propionic acid fermentation. Proc. Natl. Acad. Sci. U.S.A. 46:28-41.
1961
Tracer studies on the mechanism of carbohydrate metabolism. In Symposium on the Use of Radioisotopes in Animal Biology and the Medical Sciences, pp 193-203. New York: Academic Press.
With L. G. Ljungdahl, E. Racker, and D. Couri. Formation of unequally labeled fructose-6-phosphate by an exchange reaction catalyzed by transaldolase. J. Biol. Chem. 236:1622-25.
With P. M. L. Siu and R. L. Stjernholm. Fixation of CO2 by phosphoenolpyruvic carboxytrans-phosphorylase. J. Biol. Chem. 236:PC21-22.
With R. L. Stjernholm. Transcarboxylase. II. Purification and properties of methylmalonyl-oxalacetic transcarboxylase. Proc. Natl. Acad. Sci. U.S.A. 47:289-303.
With R. L. Stjernholm. Methylmalonyl isomerase. II. Purification and properties of the enzymes from Propionibacteria. Proc. Natl. Acad. Sci. U.S.A. 47:303-13.
1962
With R. G. Hansen, G. J. Peeters, B. Jacobson, and J. Wilken. Lactose synthesis. VI. Labeling of lactose precursors by glycerol-1,3-C14 and glucose-2-C14. J. Biol. Chem. 237:1034-39.
With R. W. Kellermeyer. Methylmalonyl isomerase: a study of the mechanism of isomerization. Biochemistry 1:1124-31.
With I. A. Rose, R. W. Kellermeyer, and R. L. Stjernholm. The distribution of C14 in glycogen from deuterated glycerol-C14 as a measure of the effectiveness of triosephosphate isomerase in vivo. J. Biol. Chem. 237:3325-31.
With P. M. L. Siu. Phosphoenolpyruvic carboxytransphosphorylase, a CO2 fixation enzyme from propionic acid bacteria. J. Biol. Chem. 237:3044-51.
With R. L. Stjernholm. Assimilation of carbon dioxide by heterotrophic organisms. In The Bacteria: A Treatise on Structure and Function, ed. I. Gunsalus and R. Stanier. New York: Academic Press.
1963
With S. H. Allen, R. Kellermeyer, R. L. Stjernholm, and B. Jacobson. The isolation, purification and properties of methylmalonyl racemase. J. Biol. Chem. 238:1637-42.
With S. H. Allen and R. L. Stjernholm. The noninvolvement of the ureido carbon of biotin in transcarboxylation. J. Biol. Chem. 238:PC2889-91.
With S. H. Allen, R. L. Stjernholm, and B. Jacobson. Transcarboxylase purification and properties of methyl-malonyl-oxaloacetic trans-carboxylase containing tritiated biotin. J. Biol. Chem. 238:547-56.
With J. Katz. The use of C14O2 yields from glucose-l- and 6-C14 for the evaluation of the pathways of glucose metabolism. J. Biol. Chem. 238:517-23.
With J. Katz and B. R. Landau. Estimation of pathways of carbohydrate metabolism. Biochem. Z. 338:809-47.
With H. Lochmuller, C. Riepertinger, and F. Lynen. Transcarboxylase. IV. Function of biotin and the structure and properties of the carboxylated enzyme. Biochem. Z. 337:247-66.
With R. L. Stjernholm. The symmetrical C3 in the propionic acid fermentation and the effect of avidin on propionate formation. Iowa State Coll. J. Sci. 38:123-40
1964
With S. H. Allen, R. W. Kellermeyer, and R. L. Stjernholm. Purification and properties of enzymes involved in the propionic acid formation. J. Bacteriol. 87:171-87.
With J. Katz and B. Landau. Evaluation of metabolic pathways of glucose. Abstracts, Sixth International Congress of Biochemistry, vol. 4, pp. 495-96.
With R. W. Kellermeyer, S. H. Allen, and R. L. Stjernholm. Methylmalonyl isomerase. IV. Purification and properties of the enzyme from Propionibacteria. J. Biol. Chem. 239:2562-69.
With R. W. Kellermeyer, R. L. Stjernholm, and S. H. Allen. Metabolism of methylmalonyl-CoA and the role of biotin and B12 coenzymes. Ann. N.Y. Acad. Sci. 112:661-79.
With B. Landau, G. Bartsch, and J. Katz. Estimation of pathway contributions to glucose metabolism and the rate of isomerization of hexose-6-phosphate. J. Biol. Chem. 239:686-96.
1965
Incorporation of C14 from carbon dioxide into sugar phosphates, carboxylic acids and amino acids by Clostridium thermoaceticum. J. Bacteriol. 89:1055-64.
With L. G. Ljungdahl and E. Irion. Total synthesis of acetate from CO2. I. Co-methylcobyric acid and Co-(methyl)-5-methoxy-benzimidazolyl-cobamide as intermediates with Clostridium thermoaceticum. Biochemistry 4:2771-80.
With G. J. Peeters, R. Verbeke, M. Lauryssens, and B. Jacobson. Estimation of the pentose cycle in the perfused cow's udder. Biochem. J. 96:607-15.
With M. F. Utter. The role of CO2 fixation in metabolism. Essays Biochem. 1:1-27.
1966
With J. J. Davis and H. Lochmuller. The equilibria reactions catalyzed by carboxytransphosphorylase, carboxykinase and pyruvate carboxylase and the synthesis of p-enolpyruvate. J. Biol. Chem. 241:5692-5704.
With L. Li and L. G. Ljungdahl. Properties of nicotinamide adenine dinucleotide phosphate-dependent formate dehydrogenase from C. thermoaceticum. J. Bacteriol. 92:405-12.
With H. Lochmuller and J. J. Davis. Phosphoenolpyruvate carboxy-transphosphorylase. II. Crystallization and properties. J. Biol. Chem. 241:5678-91.
1967
With L. G. Ljungdahl. The role of corrinoids in the total synthesis of acetate from CO2. In Seventh International Congress of Biochemistry, Tokyo, Colloqium XII, pp. 549-50.
1968
Mechanism of formation of oxalacetate and phosphoenolpyruvate from pyruvate. J. Vitamins 14:59-67.
With S. H. Allen and R. W. Kellermeyer. Methylmalonyl-CoA racemase from propionibacterium shermanii. Methods Enzymol. 13:194-98.
With T. G. Cooper, T. Tchen, and C. Benedict. The carboxylation of phosphoenolpyruvate and pyruvate. I. The active species of "CO2" utilized by phosphoenolpyruvate carboxykinase, carboxy-transphosphorylase and pyruvate carboxylase. J. Biol. Chem. 243:3857-63.
With J. J. Davis and J. M. Willard. Phosphoenolpyruvate carboxy-phosphorylase from Propionibacterium shermanii. Methods Enzymol. 13:297-309.
With H. Evans. The mechanism of the pyruvate phosphate dikinase reaction. Proc. Natl. Acad. Sci. U.S.A. 61:1448-53.
With B. Jacobson, B. Gervin, and D. Northrop. Oxalacetate transcarboxylase from Propionibacterium. Methods Enzymol. 13:215-31.
With R. W. Kellermeyer. 2-methylmalonyl-CoA mutase from Propioni-bacterium shermanii. Methods Enzymol. 13:207-15.
1969
With T. G. Cooper, T. Tchen, C. Benedict, and D. Filmer. The species of "CO2" utilized in the carboxylation of P-enolpyruvate and pyruvate. In Chemistry, Biochemistry, and Physiological Aspects, pp. 183-92. Washington: National Aeronautics and Space Administration.
With J. J. Davis and J. M. Willard. Phosphoenolpyruvate carboxy-transphosphorylase. III. Comparison of the fixation of CO2 and the conversion of phosphoenolpyruvate and phosphate to pyruvate and pyrophosphate. Biochemistry 8:3127-36.
With J. J. Davis and J. M. Willard. Phosphoenolpyruvate carboxy-transphosphorylase. V. Mechanism of the reaction and role of metal ions. Biochemistry 8:3145-55.
With B. Gerwin and B. Jacobson. Transcarboxylase. VIII. Isolation and properties of a biotin-carboxyl carrier protein. Proc. Natl. Acad. Sci. U.S.A. 64:1315-22.
With L. G. Ljungdahl. Total synthesis of acetate from CO2 by heterotrophic bacteria. Ann. Rev. Microbiol. 23:515-38.
With D. Northrop. Transcarboxylase. V. The presence of bound zinc and cobalt. J. Biol. Chem. 244:5801-7.
With D. Northrop. Transcarboxylase. VII. Exchange reactions and kinetics of oxalate inhibition. J. Biol. Chem. 244:5820-27.
With I. A. Rose, E. L. O'Connell, P. Noce, M. F. Utter, J. M. Willard, T. G. Cooper, and M. Benziman. Stereochemistry of the enzymatic carboxylation of phosphoenolpyruvate. J. Biol. Chem. 244:6130-33.
With A. Y. Sun and L. G. Ljungdahl. Total synthesis of acetate from CO2. II. Purification and properties of formyltetrahydrofolate synthetase from Clostridium thermoaceticum. J. Bacteriol. 98:842-44.
With J. M. Willard and J. J. Davis. Phosphoenolpyruvate carboxy-transphosphorylase. IV. Requirement of metal cations. Biochemistry 8:3137-44.
1970
With F. Ahmad and B. Jacobson. Transcarboxylase. X. Assembly of active transcarboxylase from its inactive subunits and incorporation of the biotin-carboxyl carrier protein. J. Biol. Chem. 245:6486-88.
With B. Jacobson, B. Gerwin, F. Ahmad, and P. Waegell. Trans-carboxylase. IX. Parameters effecting dissociation and reassociation of the enzyme. J. Biol. Chem. 245:6471-83.
1971
Biochemistry. Fed. Proc. 30:1715-18.
With T. G. Cooper. The carboxylation of phosphoenolpyruvate and pyruvate. II. The active species of "CO2" utilized by phosphoenolpyruvate carboxylase and pyruvate carboxylase. J. Biol. Chem. 246:5488-90.
With H. Evans. Purification and properties of pyruvate phosphate dikinase from propionic acid bacteria. Biochemistry 10:721.
With R. Ghambeer, M. Schulman, and L. G. Ljungdahl. Total synthesis of acetate from CO2. III. Inhibition by alkylhalides of the synthesis from CO2, methyltetrahydrofolate and methyl-B12 by Clostridium thermoaceticum. Arch. Biochem. Biophys. 143:471-84.
With R. A. Harte. International structures in science. Fed. Proc. 30:1713-14.
With D. Parker and T. Wu. Total synthesis of acetate from CO2: methyltetrahydrofolate, an intermediate and a procedure for separation of the folates. J. Bacteriol. 108:770-76.
With M. Schulman. Determination and degradation of microquantities of acetate. Anal. Biochem. 39:505-20.
1972
Some comments about teaching biochemistry. Biochem. Ed. 1:2-3.
Transcarboxylase. In The Enzymes, 3rd ed., ed. P. Boyer. pp. 83-113. New York: Academic Press.
My life and carbon dioxide fixation. In The Molecular Basis of Biological Transport, Miami Winter Symposium, vol. 3, pp. 1-54.
With F. Ahmad, D. H. Lygre, and B. Jacobson. Transcarboxylase. XII. Identification of the metal-containing subunits of transcarboxylase and stability of the binding. J. Biol. Chem. 247:6299-6305.
With N. M. Green, R. C. Valentine, N. H. Wrigley, F. Ahmad, B. Jacobson. Transcarboxylase. XI. Electron microscopy and subunit structure. J. Biol. Chem. 247:6284-98.
With M. E. Haberland and J. M. Willard. Phosphoenolpyruvate carboxytransphosphorylase: Study of the catalytic and physical structures. Biochemistry 11:712-22.
With Y. Milner. Isolation of pyrophosphoryl form of pyruvate, phosphate dikinase from Propionibacteria. Proc. Natl. Acad. Sci. U.S.A. 69:2463-68.
With D. J. Parker, R. K. Ghambeer, and L. G. Ljungdahl. Total synthesis of acetate from carbon dioxide. Retention of deuterium during carboxylation of trideuteriomethyltetrahydrofolate or trideuteriomethylcobalamin. Biochemistry 11:3074-80.
With M. Schulman, D. J. Parker, and L. G. Ljungdahl. Total synthesis of acetate from CO2. V. Determination by mass analysis of the different types of acetate formed from 14CO2 by heterotrophic bacteria. J. Bacteriol. 109:633-44.
1973
The Activities of the International Union of Biochemistry. Information Bulletin for 9th International Congress of Biochemistry, Stockholm, pp. 13-17.
With F. Ahmad, B. Jacobson, N. M. Green, and N. Wrigley. Transcarboxylase: A biotinyl-metallo-enzyme with a unique structure. In Proceedings of 8th Meeting of Federation of European Biochemistry Society, Enzymes: Structure and Function, vol. 29, pp. 201-16.
With R. K. Ghambeer and L. G. Ljungdahl. Total synthesis of acetate from CO2. VII. Evidence with Clostridium thermoaceticum that the carboxyl of acetate is derived from the carboxyl of pyruvate by transcarboxylation and not by fixation of CO2. J. Biol. Chem. 248:6255-61.
With W. E. O'Brien and R. Singleton, Jr. Phosphoenolpyruvate carboxytransphosphorylase. An investigation of the mechanism with 18O. Biochemistry 12:5247-52.
1974
With W. E. O'Brien. Carboxytransphosphorylase. VIII. Ligand- mediated interaction of subunits as a possible control mechanism in Propionibacteria. J. Biol. Chem. 249:4917-25.
1975
Appendix VIII to the discovery of carbon dioxide fixation in mammalian tissues (by Krebs). Mol. Cell. Biochem. 5:91-94.
With F. Ahmad, B. Jacobson, M. Chuang, and W. Brattin. Isolation of the subunits of transcarboxylase and reconstitution of the active enzyme from the subunits. J. Biol. Chem. 250:918-26.
With F. Ahmad, B. Jacobson, M. Chuang, and W. Brattin. Isolation of peptides from the carboxyl carrier subunit of transcarboxylase. Role of the non-biotinyl peptide in assembly. Biochemistry 14:1606-11.
With M. Berger. Purification of the subunits of transcarboxylase by affinity chromatography on avidin-sepharose. J. Biol. Chem. 250:927-33.
With M. Chuang, F. Ahmad, and B. Jacobson. Evidence that the two partial reactions of transcarboxylation are catalyzed by two dissimilar subunits of transcarboxylase. Biochemistry 14:1611-19.
With Y. Milner and G. Michaels. Pyruvate, orthophosphate dikinase of Bacteroides OSUS and Propionibacterium shermanii. Methods Enzymol. 42:199-212.
With W. E. O'Brien and S. Bowien. Isolation and characterization of a pyrophosphate-dependent phosphofructokinase from Propioni-bacterium shermanii. J. Biol. Chem. 250:8690-95.
With M. Schulman. Enzymatic determination of microquantities of acetate. Methods Enzymol. 35:298-301.
With M. Schulman. Succinyl-CoA: propionate CoA transferase from Propionibacterium shermanii. Methods Enzymol. 35:235-42.
1976
The reactive group of biotin in catalysis by biotin enzymes. Trends Biochem. Sci. 1:4-6.
Subunit-subunit interactions of transcarboxylase. Fed. Proc. 35:1899-1907.
Reflections on Lynen's laboratory in Die Aktivierte Essigsaure und ihre Folgen. Autobiographische Beitrage von Schulem und Freunded Feodor Lynens, ed. G. Hartmann. Berlin: Walter de Gruyter.
International responsibilities. Trends Biochem. Sci. 1:49-50.
Trailing the propionic acid bacteria. In Reflections on Biochemistry: A Symposia in Honor of Severo Ochoa, ed. A. Kornberg, B. L. Horecker, L. Cornudella, and J. Oro. New York: Pergamon Press.
With M. Berger. Immunochemistry of the subunits of transcarboxylase. J. Biol. Chem. 251:7021-33.
With Y. Milner. Steady state exchange kinetics. J. Biol. Chem. 251:7920-28.
With A. M. Spronk and H. Yoshida. Isolation of 3-phosphohistidine from phosphoryl pyruvate, phosphate dikinase. Proc. Natl. Acad. Sci. U.S.A. 73:4415-19.
With G. K. Zwolinski. Transcarboxylase: role of biotin, metals, and subunits in the reaction and its quaternary structure. Crit. Rev. Biochem. 4:47-122.
1977
Some reactions in which inorganic pyrophosphate replaces ATP and serves as a source of energy. Fed. Proc. 36:2197-2206.
With R. E. Barden. Biotin enzymes. Ann. Rev. Biochem. 46:385-413.
With J. Chiao and E. M. Poto. A new large form of transcarboxylase with six peripheral subunits and twelve biotinyl carboxyl carrier subunits. J. Biol. Chem. 252:1490-99.
With E. M. Poto. The association-dissociation of transcarboxylase. Biochemistry 16:1949-55.
With W. E. O'Brien and G. Michaels. Properties of carboxy-transphosphorylase; pyruvate, phosphate dikinase; PPi-phospho-fructokinase and PPi-acetate kinase and their roles in the metabolism of inorganic pyrophosphate. Adv. Enzymol. 45:85-155.
With N. H. Wrigley and J. Chiao. Electron microscopy of the large form of transcarboxylase with six peripheral subunits. J. Biol. Chem. 252:1500-04.
With G. K. Zwolinski, B. Bowien, and F. Harmon. The structure of the subunits of transcarboxylase and their relationship to the quaternary structure of transcarboxylase. Biochemistry 16:4627-37.
1978
With G. A. Cook, W. E. O'Brien, M. T. King, and R. Veech. A rapid, enzymatic assay for the measurement of inorganic pyrophosphate in animal tissue. Anal. Biochem. 91:557-65.
With G. Michaels, Y. Milner, and B. R. Moskovitz. Pyruvate phosphate dikinase. Metal requirements and inactivation of the enzyme by sulfhydryl agents. J. Biol. Chem. 253:7656-61.
With Y. Milner and G. Michaels. Pyruvate, phosphate dikinase of Bacteroides symbiosus. Catalysis of partial reactions and formation of phosphoryl and pyrophosphoryl forms of the enzyme. J. Biol. Chem. 253:878-83.
With B. R. Moskovitz. Requirement of monovalent cations for enolization of pyruvate by pyruvate, phosphate dikinase. J. Biol. Chem. 253:884-88.
With E. M. Poto, R. E. Barden, and E. P. Lau. Photoaffinity labeling and stoichiometry of the coenzyme A ester sites of transcarboxylase. J. Biol. Chem. 253:2979-83.
With F. K. Welty. Purification of the "corrinoid" enzyme involved in the synthesis of acetate by Clostridium thermoaceticum. J. Biol. Chem. 253:5832-38.
With H. Yoshida. Crystalline pyruvate, phosphate dikinase from Bacteroides symbiosus. Modification of essential histidyl residues and bromopyruvate inactivation. J. Biol. Chem. 253:7650-55.
1979
Obituary--Feodor (Fitzi) Lynen. Trends Biochem. Sci. 4:300-2.
The anatomy of transcarboxylase and the role of its subunits. Crit. Rev. Biochem. 7:143-60.
The role of corrinoids in the total synthesis of acetate from CO2. In Vitamin B12, ed. B. Zagalak and W. Friedrich. Berlin: Walter de Gruyter.
With H. L. Drake and N. H. Goss. A new, convenient method for the rapid analysis of inorganic pyrophosphate. Anal. Biochem. 94:117-20.
With W. L. Maloy, B. U. Bowien, G. K. Zwolinski, K. G. Kumar, L. H. Ericsson, and K. A. Walsh. Amino acid sequence of the biotinyl subunit from transcarboxylase. J. Biol. Chem. 254:11615-22.
With L. J. Waber. Mechanism of acetate synthesis from CO2 by Clostridium acidiurici. J. Bacteriol. 140:468-78.
1980
IUB and the person. Trends Biochem. Sci. 4:I-II.
With H. L. Drake and S. Hu. Purification of carbon monoxide dehydrogenase, a nickel enzyme from Clostridium thermoaceticum. J. Biol. Chem. 255:7174-80.
With C. T. Evans and N. H. Goss. Pyruvate, phosphate dikinase: affinity labeling of the adenosine 5´-triphosphate-adenosine 5´-monophosphate site. Biochemistry 19:5809-14.
With N. H. Goss and C. T. Evans. Pyruvate, phosphate dikinase: sequence of the histidyl peptide, the pyrophosphoryl and phosphoryl carrier. Biochemistry 19:5805-9.
With F. R. Harmon, M. Berger, H. Beegen, and N. Wrigley. Transcarboxylase: an electron microscopic study of the enzyme with antibodies to biotin. J. Biol. Chem. 255:9458-64.
With F. R. Harmon, B. Wuhr, K. Hubner, and F. Lynen. Comparison of the biotination of apotranscarboxylase and its aposubunits. Is assembly essential for biotination? J. Biol. Chem. 255:7397-7409.
1981
Obituary, Merton F. Utter. Trends Biochem. Sci. 6:V-VI.
Metabolic cycles in the fermentation of propionic acid bacteria. In Current Topics in Cellular Regulation, vol. 18, ed. R. Estabrook and P. Srere. New York: Academic Press.
With C. Bahler, N. Goss, and E. Poto. Transcarboxylase: dissociation and reassociation of the central hexameric subunit. Biochem. Intl. 3:349-58.
With H. L. Drake and S. Hu. Purification of five components from Clostridium thermoaceticum which catalyzes synthesis of acetate from pyruvate and methyltetrahydrofolate. Properties of phospho-transacetylase. J. Biol. Chem. 256:11137-44.
1982
From CO2 to acetate. In From Cyclotrons to Cytochromes: Essays in Molecular Biology and Chemistry, ed. N. O. Kaplan and A. Robinson. New York: Academic Press.
The discovery of the fixation of CO2 by heterotrophic organisms and metabolism of the propionic acid bacteria. In Of Oxygen, Fuels, and Living Matter; Part 2, ed. G. Semenza. New York: John Wiley & Sons.
With H. L. Drake and S. Hu. Studies with Clostridium thermoaceticum and the resolution of the pathway used by acetogenic bacteria that grow on carbon monoxide or carbon dioxide and hydrogen. In Proceedings Biochemistry Symposium, ed. E. S. Snell. Annual Reviews.
With N. H. Goss. Covalent chemistry of pyruvate, orthophosphate dikinase. Methods Enzymol. 87:51-66.
With F. R. Harmon and N. H. Goss. Stabilization of the quaternary structure of transcarboxylase by cobalt(II) ions. Biochemistry 21:2847-52.
With J. P. Hennessey, W. C. Johnson, and C. Bahler. Subunit interactions of transcarboxylase as studied by circular dichroism. Biochemistry 21:642-46.
With S. Hu and H. L. Drake. Synthesis of acetyl coenzyme A from carbon monoxide, methyltetrahydrofolate, and coenzyme A by enzymes from Clostridium thermoaceticum. J. Bacteriol. 149:440-48.
With G. K. Kumar. Intrinsic fluorescence of transcarboxylase during subunit-subunit interactions. Biochem. Intl. 4:605-16.
With G. K. Kumar, C. R. Bahler, and R. B. Merrifield. The amino acid sequences of the biotinyl subunit essential for the association of transcarboxylase. J. Biol. Chem. 257:13828-34.
With L. G. Ljungdahl. Acetate Biosynthesis Vitamin B12, vol. 2, ed. D. Dolphin. New York: John Wiley & Sons.
With W. J. Whelan. Freedom to meet. Trends Biochem. Sci. 7:351.
1983
With B. R. Landau. The pentose cycle in animal tissues: evidence for the classical and against the 'L-type' pathway. Trends Biochem. Sci. 8:292-96.
With N. F. Phillips and N. H. Goss. Modification of pyruvate, phosphate dikinase with pyridoxal 5´-phosphate: evidence for a catalytically critical lysine residue. Biochemistry 22:2518-23.
1984
With N. H. Goss. Formation of N-(biotinyl)lysine in biotin enzymes. Methods Enzymol. 107:261-78.
With S. Hu and E. Pezacka. Acetate synthesis from carbon monoxide by Clostridium thermoaceticum. Purification of the corrinoid protein. J. Biol. Chem. 259:8892-97.
With E. Pezacka. Role of carbon monoxide dehydrogenase in the autotrophic pathway used by acetogenic bacteria. Proc. Natl. Acad. Sci. U.S.A. 81:6261-65.
With E. Pezacka. The synthesis of acetyl-CoA by Clostridium thermoaceticum from carbon dioxide, hydrogen, coenzyme A and methyltetra-hydrofolate. Arch. Microbiol. 137:63-69.
With N. A. Robinson and N. H. Goss. Polyphosphate kinase from Propionibacterium shermanii: formation of an enzymatically active insoluble complex with basic proteins and characterization of synthesized polyphosphate. Biochem. Intl. 8:757-69.
1985
The role of the International Union of Biochemistry (IUB). BioEssays 3:42-44.
Then and now. Ann. Rev. Biochem. 54:1-41.
Inorganic pyrophosphate and polyphosphates as sources of energy. Curr. Top. Cell. Regul. 26:355-69.
With D. V. Craft, N. H. Goss, and N. Chandramouli. Purification of biotinidase from human plasma and its activity on biotinyl peptides. Biochemistry 24:2471-76.
With N. H. Goss. Phosphorylation enzyme of the propionic acid bacteria and the roles of ATP, inorganic pyrophosphate, and polyphosphates. Proc. Natl. Acad. Sci. U.S.A. 82:312-15.
With G. K. Kumar. Transcarboxylase: its quaternary structure and the role of the biotinyl subunit in the assembly of the enzyme and in catalysis. Ann. N.Y. Acad. Sci. 447:1-22.
With G. K. Kumar and H. Beegen. Assembly of subunits and structure of transcarboxylase: sequence requirement and electron microscopy of crystals. Ann. N.Y. Acad. Sci. 447:403-5.
With S. W. Ragsdale. Acetate biosynthesis by acetogenic bacteria. Evidence that carbon monoxide dehydrogenase is the condensing enzyme that catalyzes the final steps of the synthesis. J. Biol. Chem. 260:3970-77.
With S. W. Ragsdale and W. E. Antholine. Evidence that an iron-nickel-carbon complex is formed by reaction of CO with the CO dehydrogenase from Clostridium thermoaceticum. Proc. Natl. Acad. Sci. U.S.A. 82:6811-14.
1986
The synthesis of lactose and related investigations. Vlaams Diergeneeskd. Tijdschr. 55:274-85.
With J. E. Clark and H. Beegen. Isolation of intact chains of polyphosphate from Propionibacterium shermanii grown on glucose or lactate. J. Bacteriol. 168:1212-19.
With C. Pepin. Polyphosphate glucokinase from Propionibacterium shermanii. Kinetics and demonstration that the mechanism involves both processive and nonprocessive type reactions. J. Biol. Chem. 261:4476-80.
With C. A. Pepin and N. A. Robinson. Determination of the size of polyphosphates with polyphosphate glucokinase. Biochem. Intl. 12:111-23.
With E. Pezacka. The autotrophic pathway of acetogenic bacteria. Role of CO dehydrogenase disulfide reductase. J. Biol. Chem. 261:1609-15.
With N. F. B. Phillips. Isolation of pyrophosphohistidine from pyrophosphorylated pyruvate, phosphate dikinase. Biochemistry 25:1644-49.
With S. W. Ragsdale and E. Pezacka. The acetyl-CoA pathway: a newly discovered pathway of autotrophic growth. Trends Biochem. Sci. 11:14-18.
With S. W. Ragsdale and E. Pezacka. A new pathway of autotrophic growth utilizing carbon monoxide or carbon dioxide and hydrogen. Biochem. Intl. 12:421-40.
With S. W. Ragsdale and E. Pezacka. The acetyl-CoA pathway of autotrophic growth. FEMS Microbiol. Rev. 39:345-62.
With N. A. Robinson. Polyphosphate kinase from Propionibacterium shermanii. Demonstration that the synthesis and utilization of polyphosphate is by a processive mechanism. J. Biol. Chem. 261:4481-85.
With E. Skrzpczak-Jankum, A. Tulinsky, J. P. Fillers, and K. G. Kumar. Preliminary crystallographic data and quaternary structural implications of the central subunit of the multi-subunit complex transcarboxylase. J. Mol. Biol. 188:495-98.
1987
With J. E. Clark. Preparation of standards and determination of sizes of long-chain polyphosphates by gel electrophoresis. Anal. Biochem. 161:280-90.
With C. A. Pepin. The mechanism of utilization of polyphosphate by polyphosphate glucokinase from Propionibacterium shermanii. J. Biol. Chem. 262:5223-26.
With N. A. Robinson and J. E. Clark. Polyphosphate kinase from Propionibacterium shermanii. Demonstration that polyphosphates are primers and determination of the size of the synthesized polyphosphate. J. Biol. Chem. 262:5216-22.
With N. A. Robinson, C. Pepin, and J. E. Clark. Polyphosphate kinase and polyphosphate glucokinase of Propionibacterium shermanii. In Phosphate Metabolism and Cellular Regulation in Microorganisms, ed. A. Torriani-Gorini and F. C. Rothman. Washington, D.C.: American Society for Microbiology.
1988
Squiggle phosphate of inorganic pyrophosphate and polyphosphates. In The Roots of Modern Biochemistry, ed. H. Kleinkauf, H. von Döhren, and L. Jaenicke. Berlin: Walter de Gruyter.
With J. E. Clark. Biological aspects of inorganic polyphosphates. Ann. Rev. Biochem. 57:235-60.
With G. K. Kumar and H. Beegen. Involvement of tryptophans at the catalytic and subunit-binding domains of transcarboxylase. Biochemistry 27:5972-78.
With G. K. Kumar, F. C. Haase, and N. F. Phillips. Involvement and identification of a tryptophanyl residue at the pyruvate binding site of transcarboxylase. Biochemistry 27:5978-83.
With E. Pezacka. Acetyl-CoA pathway of autotrophic growth. Identification of the methyl-binding site of the CO dehydrogenase. J. Biol. Chem. 263:16000-06.
With S. W. Ragsdale, T. A. Morton, L. G. Ljungdahl, and D. V. DerVartanian. Nickel in CO dehydrogenase. In The Bioinorganic Chemistry of Nickel, ed. J. R. Lancaster, Jr. New York: VCH Publishers.
With D. Samols, C. G. Thornton, V. L. Murtif, G. K. Kumar, and F. C. Haase. Evolutionary conservation among biotin enzymes. J. Biol. Chem. 263:6461-64.
With T. Shanmugasundaram and G. K. Kumar. Involvement of tryptophan residues at the coenzyme A binding site of carbon monoxide dehydrogenase from Clostridium thermoaceticum. Biochemistry 27:6499-6503.
With T. Shanmugasundaram and S. W. Ragsdale. Role of carbon monoxide dehydrogenase in acetate synthesis by the acetogenic bacterium, Acetobacterium woodii. BioFactors 1:147-52.
With B. Shenoy. Purification and properties of the synthetase catalyzing the biotination of the aposubunit of transcarboxylase from Propionibacterium shermanii. FASEB J. 2:2396-2401.
1989
Past and present of CO2 utilization. In Autotrophic Bacteria, ed. H. G. Schlegel and B. Bowien. New York: Springer-Verlag.
With T. Shanmugasundaram, G. K. Kumar, and B. C. Shenoy. Chemical modification of the functional arginine residues of carbon monoxide dehydrogenase from Clostridium thermoaceticum. Biochemistry 28:7112-16.
1991
Life with CO or CO2 and H2 as a source of carbon and energy. FASEB J. 5:156-63.
With L. G. Ljungdahl. Autotrophic character of the acetogenic bacteria. In Variations in Autotrophic Life, ed. J. M. Shively and L. L. Barton. New York: Academic Press.
With T. A. Morton, J. A. Runquist, S. W. Ragsdale, T. Shanmugasundaram, and L. G. Ljungdahl. The primary structure of the subunits of carbon monoxide dehydrogenase/acetyl-CoA synthase from Clostridium thermoaceticum. J. Biol. Chem. 266:23824-28.
With T. Shanmugasundaram. Interaction of ferredoxin with carbon monoxide dehydrogenase from Clostridium thermoaceticum. J. Biol. Chem. 267:897-900.
1992
With B. C. Shenoy, Y. Xie, V. L. Park, G. K. Kumar, H. Beegen, and D. Samols. The importance of methionine residues for the catalysis of the biotin enzyme, transcarboxylase. Analysis by site-directed mutagenesis. J. Biol. Chem. 267:18407-12.
1993
With S. B. Woo, B. C. Shenoy, W. J. Magner, G. K. Kumar, H. Beegen and D. Samols. Effect of deletion from the carboxyl terminus of the 12S subunit of activity of transcarboxylase. J. Biol. Chem. 268:16413-19.
With C. G. Thornton, G. K. Kumar, F. C. Haase, N. F. B. Phillips, S. B. Woo, V. M. Park, W. J. Magner, S. B. Shenoy and D. Samols. Primary structure of the monomer of the 12S subunit of transcarboxylase as deduced from DNA and characterization of the product expressed in Escherichia coli. J. Bacteriol. 175:5301-8.
With C. G. Thornton, G. K. Kumar, B. C. Shenoy, F. C. Haase, N. F. B. Phillips, V. M. Park, W. J. Magner, D. P. Hejlik and D. Samols. Primary structure of the 5S subunit of transcarboxylase as deduced from the genomic DNA sequence. FEBS Lett. 330:191-96.
With N. F. B. Phillips and P. J. Horn. The polyphosphate and ATP-dependent glucokinase from Propionibacterium shermanii: both activities are catalyzed by the same protein. Arch. Biochem. Biophys. 300:309-19.

Biographical Memoirs National Academy of Sciences