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HARLAN D GOFF WOOD
September 2, ~ 907-September I 2, ~ 99'
BY DAVID A. GOLDTHWAIT AND
RI C HARD W. HAN S O N
HARLAND GOFF WOOD, WHO was clescenclec! from William
Goffe (b. 1619), one of the appointee! judges respon-
sible for the beheading of King Charles I, was born on
September 2, 1907, in the small town of Delavan, Minne-
sota. His parents, both of whom hac! only a high school
education, taught their four sons en c! one daughter to work
hare! en c! to be self-reliant the result for the sons: two
Ph.D.s, one Ph.D.-M.D., one M.D., en c! one LL.B, en c! for
the daughter: an honorary LL.D. It is h are! to picture HarIanc!
Wool! as a frail chiTc! 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 en c! then
running back after lunch. At Macalester College in Minne-
sota, he majorec! in chemistry en c! there met Milcirec! Davis,
whom he marries! in 1929. In 1931 he was acceptec! 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 Harianc!
made his stunning discovery of CO2 fixation, which up to
that time was known to occur only in chemosynthetic en c!
photosynthetic autotrophs. This idea was so controversial
395
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B I O G RA P H I C A L
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that for some time Professor Werkman cloubtec! the vaTiclity
of HarIancl's finclings.
From 1935 to 1936 HarIanc! worker! as a fellow with W.
H. Petersen at the University of Wisconsin, en c! it was here
that he joiner! Ec! Tatum in studying the growth factor re-
quirements for propionibacteria. HarIanc! returnee! to
Werkman's department in 1936 to focus on CO2 fixation, as
will be cliscussecI. Although HarIanc! was tremenclously pro-
cluctive at Ames, builcling a thermal diffusion column for
the isolation of i3C as well as a mass spectrometer to mea-
sure the isotope, Werkman wouIc! not initially allow him to
work on animals en c! wouIc! not arrange for HarIancl's fu-
ture inclepenclence at Ames. An c! so in 1943 he mover! to
the Department of Physiological Chemistry at the Univer-
sity of Minnesota, en c! it was there that he user! i3C-NaHCO3
labeling of the different carbon atoms of the glucose of rat
liver glycogen to study the pathways of glucose synthesis.
In 1946 HarIanc! acceptec! the position of chairman of
the Department of Biochemistry at the School of Medicine
of what was then Western Reserve University in ClevelancI,
Ohio, on the condition, as he toIc! Dean Joseph Wearn,
that he be allowed! to go cleer hunting with his father en c!
four brothers each autumn. He lover! cluck en c! cleer hunt-
ing en c! 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 orientec! to the use of isotopic
tracers to stucly a variety of metabolic pathways. Uncler
Hariancl's direction, this young en c! energetic group, which
included future members of the National Academy of Sci-
ences, Merton Utter en c! Lester Krampitz, createc! an out-
stancling national reputation for the department. At the
local level, he was also unique. HarIanc! instituter! a policy
that all honoraria, even for participating in stucly sections,
should go into a student travel fund, since he felt that out
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HARLAN D G O FF WO O D
397
sicle activities shouic! have an intrinsic value baser! on sci-
ence en c! not on money echoes of William Goffe. Depart-
mental seminars were at noon on Saturday en c! monthly
staff meetings were hell! after that, often until 5:00 p.m.,
when they were terminatec! by telephone calls from irate
wives. There was a pooling of resources, a sharing of all
equipment, en c! a camaraderie that wouic! be clifficult to
equal in these times.
HarIanc! Wool! spent the last forty-five years of his career
at Case Western Reserve University (Western Reserve Uni-
versity merger! with Case Institute of Technology in 1968~.
He retiree! as chairman in 1965 so that he conic! have more
time for research, en c! for Harianc! this meant research at
the bench, not just at the clesk. He continues! "pouncling
the bench," as he caller! it, right up until a few clays before
his cleath on September 12, 1991. Lymphoma was cliagnosec!
four years before his cleath, he cliec! of a fall that resultec! in
a ruptures! spleen. HarIanc! hac! undergone chemothera-
peutic cycles several times, but they never significantly halted
his scientific activities. At the time of his cleath, he hell!
three grants from the National Institutes of Health, hac! a
working group of fifteen associates, en c! was writing nine
manuscripts. At the last meeting of the ASBMB that he
attenclecI, he hac! twelve posters on clisplay en c! was present
to discuss results relater! to each of them. Between his sev-
entieth birthday en c! his cleath, he publisher! ninety-six pa-
pers, all in well-respectec! journals surely a recorc! for an
"elclerly" biochemist. He is survives! by his wife MiTcirec! en c!
two daughters.
HarIanc! Wool! left a long en c! clistinguishec! recorc! in
the life sciences, beginning with his pioneering work with
C. H. Werkman at Iowa State College, which clemonstratec!
for the first time that CO2 is utilizer! in heterotrophic or-
ganisms. In 1935 he demonstrated that the prevailing dogma
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B I O G RA P H I C A L
EMOIRS
that CO2 was utilizer! only by bacterial autotrophs was in-
correct. In a series of studies he cleterminec! the products
former! from the fermentation of glycerol by propionic acid
bacteria in a bicarbonate buffer system en c! caTculatec! the
carbon en c! oxiciation-recluction balances to account for the
carbon of the fermented substrate en c! to ensure that there
was a balance of the oxiciation-recluction state of substrates
en c! products. Surprisingly, more carbon was fount! in the
products than was supplied by the fermented glycerol. He
subsequently cliscoverec! that the extra carbon was clerivec!
from CO2 in the buffer en c! that oxidation balances! recluc-
tion when the recluction of CO2 was taken into account. He
proposer! that CO2 en c! pyruvate combiner! to form oxa-
lacetate, which subsequently was reclucec! to succinate. This
pyruvate-CO2 reaction became known as the WoocI-Werkman
reaction.
When isotopic tracers of carbon became available in the
late 1930s, HarIanc! was among the first to exploit isotopes
in biological studies. He was a true pioneer in cleveloping
procedures for the use of these isotopes for metabolic tracer
studies. As previously noted, he built a water-coolec! ther-
mal diffusion column in a five-story elevator shaft for the
separation of i3C isotopic carbon. HarIand was always fond
of describing the day that he found the column warped
en c! clistortec! clue to a temporary cirop in the water pres-
sure. This cirop, he finally cliscoverecI, occurrec! when the
home economics class let out en c! three toilets were flusher!
simultaneously! To measure i3C, he also built a mass spec-
trometer. His innovative work initially proviclec! evidence
that citrate was not part of the citric acid cycle because he
hac! assumer! that citrate was a symmetrical molecule. In his
characteristic manner, he later sail! in a Lynen Lecture that
even though he was wrong it was one of his "most impor-
tant contributions" to biochemistry. The studies by Wool!
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HARLAN D G O FF WO O D
399
en c! his colleagues in 1945 clearly clemonstratec! the path-
way of CO2 incorporation into specific carbon atoms of
glucose clerivec! from hepatic glycogen. HarIanc! gracluatec!
briefly from bacteria to cows, where his farm backgrounc!
helpec! in the injection of i4C glucose into the artery going
to the right udder. Subsequently, by personally milking each
sicle, he cleterminec! that lactose was synthesizec! from free
glucose rather than glucose-~-phosphate en c! that it was glu-
cose that reactec! with UDP-galactose to form lactose. In
collaboration with Joseph Katz en c! Bernarc! R. Landau,
HarIanc! also clevelopec! methods to estimate the propor-
tion of carbohydrate metabolizec! in the Penrose pathway
en c! glycolysis by studying i4C distributions in glucose and
glycogen. These latter studies were instrumental in estab-
lishing the stoichiometry of the Penrose pathway.
The overall direction of Hariancl's research over sixty years
continues! to be on CO2 fixation. During the last thirty
years of his life, he focuses! on establishing the reaction
mechanism of transcarboxylase (TC) from propionibacteria.
This is a key enzyme in the propionic acid cycle, en c! it
transfers a carboxy! group in the conversion of methy~malony!
CoA + pyruvate to propiony! CoA + oxalacetate. The en-
zyme is also extremely complex, with six iclentical central
subunits, each with two CoA-bincling sites, six climeric out-
sicle subunits each of the six with two keto acid sites, en c!
twelve small biotiny! subunits that carry the carboxy! groups
between the CoA and keto sites. The kinetics of the reac-
tion clic! not fit the acceptec! mechanisms, so Dexter Northrup,
then a student with HarIancI, proposer! a new kinetic mecha-
nism for TC that was later verifier! by Northrup en c! WoocI.
Extensive work was done on the separation of the three
subunits of TC en c! on the reconstitution of enzyme activ-
ity. Together with a number of associates, Wool! stucliec! the
quaternary structure of TC by electron microscopy, and this
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B I O G RA P H I C A L
EMOIRS
reveaTec! the "Mickey Mouse" enzyme. Using thin crystals of
the enzyme, resolution of the structure at 10 A was possible
by microscopy. The primary amino acid sequence of the
biotiny! subunit was cleterminecI, and, in collaboration with
Davic! Samols, the genes for all three subunits were clones!
en c! sequenced. At the enc! of his life, HarIanc! was studying
the enzymatic properties of a large number of mutants that
were generated in the three different subunits en c! was clo-
ing many of the enzyme assays himself. These studies were
of great interest because of the complexity of the subunit
structure of the enzyme en c! the ability to examine cliffer-
ent aspects of function.
Harianc! Wool! also cliscoverec! a novel pathway for car-
bon monoxide (CO) fixation in acetogens, a group of anaero-
bic bacteria that synthesize acetate from CO or CO2/H2.
This new pathway of autotrophic growth, clemonstratec! in
Ctostridium thermoaceticum en c! Acetobacterium woodii, cliffers
from all previously clescribec! pathways for autotrophic growth,
such as the Calvin reductive pentose cycle or the tricar-
boxylic acid cycle. Much of HarIancl's work in the area was
clone in collaboration with Lars Ljunciahl, both at Case West-
ern Reserve University and the University of Georgia. The
mechanism of this pathway involves recluction of CO2 to
methyTtetrahydrofolate and transfer of the me tiny! group to
a corrinoid protein. The me tiny! group is then transferred
to carbon monoxide clehycirogenase (CODH), CO ant!
CoASH/moleties combine with CODH, which catalyzes the
formation of acetyI-CoA from the above three groups. Thus,
CODH plays a central role in this pathway. Most of the
enzymes involves! in the various steps of the pathway were
purified to homogeneity. The availability of purified en-
zymes permitted HarIanc! en c! his collaborators to dissect
the pathway en c! define the role of each enzyme. Detailec!
studies towarc! eTuciciating the mechanism of action of CODH
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HARLAN D G O FF WO O D
401
were initiated. CODH contains six nickel, three zinc, thirty-
two iron atoms, forty-two labile sulficles en c! has three ac-
ceptor sites: one for the me tiny! group transferred from the
me tiny! corrinoic! enzyme, a CO site, en c! a CoASH site.
From ESR studies it was shown that the Ni-Fe center is
involves! in the interaction of the CO group with CODH.
Also, the me tiny! group is bounc! to a cysteine residue of
CODH. The CoASH substrate site has been characterizec!
using fluorescence spectroscopy, circular clichroism, en c!
chemical mollification. From these studies it was proposer!
that both tryptophan (s) en c! arginine (s) are involves! in the
bincling of CoASH to CODH. Even from this brief review it
is clear that Harianc! Wood, over the sixty years that he was
involves! in research, "follower! the trail of CO2."
HarIanc! Wool! was also a pioneer in studying the role of
pyropnospnate anct po~ypnospnate as energy sources. It has
long been acceptec! that the energy container! in the anhy-
dride bond of pyrophosphate is not utilized efficiently by
cells. However, HariancI, together with Nelson Phillips, shower!
this not to be true by the isolation en c! characterization of
bacterial enzymes that utilize pyrophosphate in reaction with
oxaloacetate, with phosphoenolpyruvate, and with fructose-
6-phosphate. Inorganic polyphosphates have been consicI-
erec! by others as primitive sources of energy. HarIanc! ex-
tensively stucliec! the enzymatic synthesis of polyphosphate
from ATP en c! shower! that a bacterial glucokinase utilizes
polyphosphate much more effectively than ATP in the reac-
tion with glucose. Two separate sites exist on the enzyme
for these two sources of high-energy phosphate. This en-
zyme may represent an intermediate stage of evolution from
a polyphosphate-dependent metabolism to an ATP-depen-
clent metabolism.
HarIand Wood's outstanding career was marked by many
innovations. However, what most characterizes! Harianc! was
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B I O G RA P H I C A L
EMOIRS
his scientific style. He was remarkable for several reasons.
First, one conic! always feel the sense of excitement en c!
drive that he brought to the experimental aspect of sci-
ence. The focus of the excitement was always on discovery.
Second, he continually clevelopec! en c! applier! the latest
technology to his experimental problem. There were many
jumps from fermentation balances all the way to gene se-
quencing. Finally, he was able to collaborate with others
very procluctively, particularly those with expertise in spe-
cific areas where the scientific results conic! not have been
achiever! by either group alone. The flavor of the man en c!
.
his approach to science are best captures! by HarIanc! him-
self in his autobiography in the Annual Review of Biochemis-
try in 1985.
HarIanc! Woocl's outstanding career was market! by many
innovations in other areas. As chairman of the biochemis-
try department at Western Reserve University, he lee! the
curriculum reform that resultec! in an integrates! organ-
system-basec! methoc! for teaching the first two years of mecli-
cal school, this curriculum has had a great impact on medi-
cal education nationally. He swayer! the faculty to vote for
the new curriculum with the challenge, "How clo 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 clean of sciences at Case Western Reserve
University from 1967 to 1969, en c! finally as university pro-
fessor en c! university professor emeritus from 1970 to 1991.
Harianc! Wool! was president of the American Society of
Biological Chemistry from 1959 to 1960. First as secretary-
general en c! then as president of the International Union
of Biochemistry in 1982-83, he clic! a great clear for that
organization's revitalization. He served on many study sec-
tions, en c! his strong support for younger biochemists clur-
ing his tenure on one of those stucly sections became known
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HARLAN D G O FF WO O D
403
as "The Wood Factor." He was a member of many advisory
boards and served as an editorial board member of a num-
ber of important journals. As a young member of the Edito-
rial Board of the Journal of Biological Chemistry, he was in-
strumental 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 presti-
gious awards, including the Eli Lilly Award, the Car! 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
MacaTester College, Northwestern University, the University
of Cincinnati, and Case Western Reserve University. He was
a member of the National Academy of Sciences, the Ameri-
can Academy of Arts and Sciences, and the Biochemical
Society of Japan and served on the President's Science Ad-
visory Committee under Presidents Johnson and Nixon.
In a 1985 Annual Review of Biochemistry article, Hariand
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 sci-
entists 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 flarland Wood spent in science,
he made countless friends in many countries who revered
him not just for his accomplishments but for his intellec-
tual 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
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BIOGRAPHICAL MEMOIRS
encouragement got the best out of his associates, en c! a
man who, once he macle up his mincI, wouIc! drive straight
towarc! his goal. In him one felt the warmth, strength, en c!
integrity that macle him unique en c! irreplaceable.
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EMOIRS
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 syn-
thesis of acetate from CO2. III. Inhibition by alkylhalides of the
synthesis from CO2, methyltetrahydrofolate and methyl-B~ 2 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 sepa-
ration of the folates. 7. 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 ea., ed. P. Boyer. pp. 83-113.
New York: Academic Press.
My life and carbon dioxide fixation. In The Molecular Basis of Biologi-
cal 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 sub-
unit structure. 7. Biol. Chem. 247:6284-98.
With M. E. Haberland and T. M. Willard. Phosphoenolpyruvate
carboxytransphosphorylase: Study of the catalytic and physical
structures. Biochemistry 11 :712-22.
With Y. Milner. Isolation of pyrophosphoryl form of pyruvate, phos-
phate dikinase from Propionibacteria. Proc. Natl. A cad. 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 deute-
rium during carboxylation of trideuteriomethyltetrahydrofolate
or trideuteriomethylcobalamin. Biochemistry 1 1: 3074-80.
With M. Schulman, D. J. Parker, and L. G. Ljungdahl. Total synthe-
sis of acetate from CO2. V. Determination by mass analysis of the
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HARLAN D G O FF WO O D
419
different types of acetate formed from i4CO2 by heterotrophic
bacteria. 7. Bacteriol. 109: 633-44.
1973
The Activities of the International Union of Biochemistry. Informa-
tion 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 struc-
ture. In Proceedings of 8th Meeting of Federation of European Biochem-
istry Society, Enzymes: Structure and Function, vol. 29, pp. 201-16.
With R. K. Ghambeer and L. G. Ljungdahl. Total synthesis of ac-
etate 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. 7. Biol. Chem.
248:6255-61.
With W. E. O'Brien and R. Singleton, Jr. Phosphoenolpyruvate
carboxytransphosphorylase. An investigation of the mechanism
with 180. Biochemistry 12:5247-52.
1974
With W. E. O'Brien. Carboxytransphosphorylase. VIII. Ligand- me-
diated interaction of subunits as a possible control mechanism in
Propionibacteria. I. Biol. Chem. 249:4917-25.
1975
Appendix VIII to the discovery of carbon dioxide fixation in mam-
malian 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 ac-
tive enzyme from the subunits. 7. 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-
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With M. Chuang, F. Ahmad, and B. Jacobson. Evidence that the two
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EMOIRS
partial reactions of transcarboxylation are catalyzed by two dis-
similar subunits of tran scarboxylase . 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. I. 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 and ihre
Folgen. Autobiographische Beitrage non Schulem and 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 T. Oro. New York: Pergamon Press.
With M. Berger. Immunochemistry of the subunits of transcarboxylase.
7. Biol. Chem. 251 :7021 -33.
With Y. Milner. Steady state exchange kinetics. 7. Biol. Chem. 251:7920-
28.
With A. M. Spronk and H. Yoshida. Isolation of 3-phosphohistidine
from phosphoryl pyruvate, phosphate dikinase. Proc. Natl. A cad.
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 ATE
and serves as a source of energy. Fed. Proc. 36:2197-2206.
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HARLAN D G O FF WO O D
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With R. E. garden. Biotin enzymes. Ann. Rev. Biochem. 46:385-413.
With T. Chiao and E. M. Poto. A new large form of transcarboxylase
with six peripheral subunits and twelve biotinyl carboxyl carrier
subunits. 7. 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 me-
tabolism of inorganic pyrophosphate. Adv. Enzymol. 45:85-155.
With N. H. Wrigley and T. Chiao. Electron microscopy of the large
form of transcarboxylase with six peripheral subunits. 7. 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 phos-
phate dikinase. Metal requirements and inactivation of the en-
zyme 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. 7. 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. garden, and E. P. Lau. Photoaffinity labeling
and stoichiometry of the coenzyme A ester sites of transcarboxylase.
7. Biol. Chem. 253:2979-83.
With F. K. Welty. Purification of the "corrinoid" enzyme involved in
the synthesis of acetate by Clostridium thermoaceticum. ]. Biol. Chem.
253:5832-38.
With H. Yoshida. Crystalline pyruvate, phosphate dikinase from Bacteroides
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Representative terms from entire chapter:
acid bacteria
