Lars G. LjungdahlProfessor of Biochemistry & Molecular BiologyGeorgia Power Distinguished Professor of Biotechnology Professor Ljungdahl received his B.S. from Stockholm Technical Institute and Ph.D. from Case Western Reserve University, Cleveland, Ohio, 1964. Dr. Ljungdahl focuses his research on the biochemistry and molecular biology of anaerobic autotrophic and acetogenic bacteria, and on anaerobic fungi and thermophilic bacteria that are able to degrade cellulose and other complex carbohydrates. The acetogenic bacteria use the acetyl-CoA pathway, also known as the Wood-Ljungdahl pathway, for carbon dioxide fixation and acetate synthesis. Work on acetogens includes the structure and function of metal centers of several enzymes involved in the acetyl-CoA pathway. An example is formate dehydrogenase, a complex metalloenzyme containing tungsten, selenium, and iron. The study of acetogens has revealed that the energy metabolism is linked to the acetyl-CoA pathway, and that they have protective mechanisms for oxygen toxicity. Both of these processes involve unique metalloenzymes, which are studied. A new acetogenic bacterium, Clostridium ljungdahlii, was named in recognition of Dr. Ljungdahl's groundbreaking research into acetogenesis. Work on anaerobic cellulolytic bacteria and fungi is concentrated on the structures of cellulosomes, which are large protein complexes containing 25 or more different polypeptides. The cellulosomes are held together by interactions of cohesins, a domain in scaffolding polypeptides, and dockerins, a domain in enzymatic subunits of the cellulosomes. This interaction is calcium dependent. The structure and function of the cellulosomes are investigated. Dr. Ljungdahl was a member of the State of Georgia Governor's Science and Technology Advisory Council from 1992 to 1996. He was elected as a foreign member of the Royal Swedish Academy of Engineering Sciences in 1987. Dr. Ljungdahl is an elected Fellow of the American Academy of Microbiology and of the American Association for the Advancement of Science. He was editor-in-chief for Applied and Environmental Microbiology from 1986 through 1995 and director of the Georgia Biotechnology Center from 1994 to 2001. He is director of the Center for Biological Resource Recovery. "Do domain interactions of glycosyl hydrolases from Clostridium thermocellum contribute to protein stability?" Kataeva, I.A.; Blum, D.L.; Li, X.-L.; Ljungdahl, L.G. Protein Engineering 2001, 14, 167-172. "A five gene cluster in Clostridium thermoaceticum encoding rubrerythrin, rubredoxin oxidoreductase, rubredoxin, type A flavoprotein, and a high molecular weight rubredoxin," Das, A.; Coulter, E.D.; Kurtz, D.M., Jr.; Ljungdahl, L.G. J. Bacteriol. 2001, 183, 1560-1567. "A dockerin-PCR-based strategy to isolate cellulosomal components of anaerobic fungi," Steenbakkers, P.J.M.; Li, X.-L.; Ximenes,E.A.; Arts, J.G.; Chen, H.; Ljungdahl, L.G.; Op den Camp, H.J.M. J. Bacteriol. 2001, 183, 5325-5333. "Structural basis for the substrate specificity of the feruloyl esterase domain of the cellulosomal xylanase Z of Clostridium thermocellum," Biochemistry. 2001, 40, 12524-12532. E-mail contact: |