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Applied and Environmental Microbiology, March 2008, p. 1447-1452, Vol. 74, No. 5
0099-2240/08/$08.00+0 doi:10.1128/AEM.01421-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

and
Naomichi Nishio*
Department of Molecular Biotechnology, Graduate School of Advanced Sciences of Matter, Hiroshima University, Kagamiyama 1-3-1, Higashi-Hiroshima 739-8530, Japan
Received 26 June 2007/ Accepted 30 November 2007
The thermophilic homoacetogenic bacterium Moorella sp. strain HUC22-1 ferments glyoxylate to acetate roughly according to the reaction 2 glyoxylate
acetate + 2 CO2. A batch culture with glyoxylate and yeast extract yielded 11.7 g per mol of cells per substrate, which was much higher than that obtained with H2 plus CO2. Crude extracts of glyoxylate-grown cells catalyzed the ADP- and NADP-dependent condensation of glyoxylate and acetyl coenzyme A (acetyl-CoA) to pyruvate and CO2 and converted pyruvate to acetyl-CoA and CO2, which are the key reactions of the malyl-CoA pathway. ATP generation was also detected during the key enzyme reactions of this pathway. Furthermore, this bacterium consumed L-malate, an intermediate in the malyl-CoA pathway, and produced acetate. These findings suggest that Moorella sp. strain HUC22-1 can generate ATP by substrate-level phosphorylation during glyoxylate catabolism through the malyl-CoA pathway.
Published ahead of print on 14 December 2007.
Present address: Department of Applied Chemistry, Graduate School of Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Naka, Koganei, Tokyo 184-8588, Japan.
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