Harland Goff Wood, September 2, 1907September 12, 1991 | By David A. Goldthwait and Richard W. Hanson | Biographical Memoirs
Harland Goff Wood
September 2, 1907 September 12,
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.
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
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.
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
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
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.
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.
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.
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.
- 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.
- With C. H. Werkman. The propionic acid
bacteria: On the mechanism of glucose dissimilation. J. Biol.
- With C. H. Werkman. Pyruvic acid in
the dissimilation of glucose by the propionic acid bacteria. Biochem.
- With C. H. Werkman. Intermediate
products of the propionic acid fermentation. Proc. Soc. Exp. Biol.
- With C. H. Werkman. The utilization
of agricultural by-products in the production of propionic acid by
fermentation. J. Agric. Res. 49:1017-20.
- With C. H. Werkman. The utilization of
CO2 by the propionic acid bacterial in the dissimilation of
glycerol. J. Bacteriol. 30:332 (Abstract).
C. H. Werkman. The isolation and possible intermediary role of
formaldehyde in the propionic acid fermentation. J. Bacteriol.
- 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.
- 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.
- With A. A. Anderson and C. H. Werkman. Growth factors for
the propionic and lactic acid bacteria. Proc. Soc. Exp. Biol. Med.
- 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.
- With C. H. Werkman and R. W.
Stone. The dissimilation of phosphate esters by the propionic acid
bacteria. Enzymologia 4:24-30.
- With A. A. Anderson and C. H. Werkman.
Nutrition of the propionic acid bacteria. J. Bacteriol.
- With C. H. Werkman. The utilization of
CO2 by the propionic acid bacteria. Biochem. J.
- With W. P. Wiggert and C. H. Werkman. The
fermentation of phosphate esters by the propionic acid bacteria.
- With R. W. Brown and C. H. Werkman. Nutrient requirements of
butyric acid butyl alcohol bacteria. J. Bacteriol. 38:631-40.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
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.
H. D. Slade, A. O. Nier, A. Hemingway, and C. H. Werkman. Assimilation
of heavy carbon dioxide by heterotrophic bacteria. J. Biol. Chem.
- 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.
- 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.
- With G. Kalnitsky and C. H. Werkman.
CO2-fixation and succinic acid formation by a cell-free
enzyme preparation of Escherichia coli. Arch. Biochem.
- With L. O. Krampitz and C. H. Werkman.
Enzymatic fixation of carbon dioxide in oxalacetate. J. Biol.
- Metabolism of nervous tissue in poliomyelitis. Lancet
- 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.
- With I. I. Rusoff and J. M. Reiner.
Anaerobic glycolysis of the brain in experimental poliomyelitis. J.
Exp. Med. 81:151-59.
- 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.
- With I. I. Rusoff. The protective action of
trypan red against infection by a neurotropic virus. J. Exp. Med.
- 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.
- 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.
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.
- 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
- 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.
- 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.
- Symposium on chemical transformation of carbons in
photosynthesis. Fed. Proc. 9:553-55.
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.
- 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.
- 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.
- 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.
- 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.
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.
- With G. Popjak. Biological asymmetry of
glycerol and formation of asymmetrically labeled glucose. J. Biol.
- With P. Schambye. The in
vivo conversion of 14C-glycerol into rat liver glycogen.
In Radioisotope Conference, vol. 1, pp. 346-50.
- Significance of
alternate pathways in the metabolism of glucose. Physiol. Rev.
- 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.
- 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.
- With R. Stjernholm and F. W. Leaver. The
metabolism of labeled glucose by the propionic acid bacteria. J.
- 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.
- 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.
- Transactions of the Third Conference
of Polysaccharides in Biology. New York: Josiah Macy, Jr.
- With I. A. Bernstein. Determination of
isotopic carbon patterns in carbohydrate by bacterial fermentation.
Methods Enzymol. 4:561-83.
- With H. Gest.
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