Biographical Memoirs Volume 69 (1996) / Chapter Skim
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HARLAND GOFF WOOD
HARLAND GOFF WOOD
Pages 394-428
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GOLDTHWAIT AND RI C HARD W HAN S O N HARLAND GOFF WOOD, WHO was clescenclec!
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i3C-NaHCO3 labeling of the different carbon atoms of the glucose of rat liver glycogen to study the pathways of glucose synthesis.
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Wool! spent the last forty-five years of his career at Case Western Reserve University (Western Reserve University merger!
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from the fermentation of glycerol by propionic acid bacteria in a bicarbonate buffer system en c! caTculatec!
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CoA + oxalacetate. The enzyme is also extremely complex, with six iclentical central subunits, each with two CoA-bincling sites, six climeric outsicle subunits each of the six with two keto acid sites, en c!
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Acetobacterium woodii, cliffers from all previously clescribec! pathways for autotrophic growth, such as the Calvin reductive pentose cycle or the tricarboxylic acid cycle.
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This enzyme may represent an intermediate stage of evolution from a polyphosphate-dependent metabolism to an ATP-depenclent metabolism. HarIand Wood's outstanding career was marked by many innovations.
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by many innovations in other areas. As chairman of the biochemistry department at Western Reserve University, he lee!
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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.
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404 BIOGRAPHICAL MEMOIRS encouragement got the best out of his associates, en c! a man who, once he macle up his mincI, wouIc!
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The aerobic dissimilation of lactic acid by the propionic acid bacteria.
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Growth factors for the propionic and lactic acid bacteria.
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Nutritive requirements of the heterofermentative lactic acid bacteria. Iowa State Coll.
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Mechanism of the butyl alcohol fermentation with heavy carbon acetic and butyric acids and acetone.
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The incorporation of acetate and butyrate carbon into rat liver glycogen by pathways other than carbon dioxide fixation.
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194:905-31. Fermentation of 3,4-Ci4 and 1-Ci4-labeled glucose by Clostridium thermoaceticum.
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The metabolism of labeled glucose by the propionic acid bacteria.
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V C14 in lactose, glycerol and serine as indicators of the triose phosphate isomerase reaction and pentose cycle.
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Trehalose and fructose as indicators of metabolism of labeled glucose by the propionic acid bacteria.
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Siu. Phosphoenolpyruvic carboxytransphosphorylase, a CO2 fixation enzyme from propionic acid bacteria.
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239:686-96. 1965 Incorporation of Ci4 from carbon dioxide into sugar phosphates, carboxylic acids and amino acids by Clostridium thermoaceticum.
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The mechanism of the pyruvate phosphate dikinase reaction.
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II. Purification and properties of formyltetrahydrofolate synthetase from Clostridium thermoaceticum.
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Purification and properties of pyruvate phosphate dikinase from propionic acid bacteria. Biochemistry 10:721.
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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.
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Michaels. Pyruvate, orthophosphate dikinase of Bacteroides OSUS and Propionibacterium shermanii.
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Michaels. Properties of carboxytransphosphorylase; pyruvate, phosphate dikinase; PPi-phosphofructokinase and PPi-acetate kinase and their roles in the metabolism of inorganic pyrophosphate.
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Hu. Purification of carbon monoxide dehydrogenase, a nickel enzyme from Clostridium thermoaceticum.
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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.
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Acetate synthesis from carbon monoxide by Clostridium thermoaceticum. Purification of the corrinoid protein.
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Acetate biosynthesis by acetogenic bacteria. Evidence that carbon monoxide dehydrogenase is the condensing enzyme that catalyzes the final steps of the synthesis.
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Polyphosphate kinase and polyphosphate glucokinase of Propionibacterium shermanii. In Phosphate Metabolism and Cellular Regulation in Microorganisms, ed.
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Chemical modification of the functional arginine residues of carbon monoxide dehydrogenase from Clostridium thermoaceticum. Biochemistry 28:7112-16.
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The primary structure of the subunits of carbon monoxide dehydrogenase/acetylCoA synthase from Clostridium thermoaceticum.
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