Electron transport chain in aerobically cultivated Zymomonas mobilis
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چکیده
منابع مشابه
Structure of the Zymomonas mobilis respiratory chain: oxygen affinity of electron transport and the role of cytochrome c peroxidase
The genome of the ethanol-producing bacterium Zymomonas mobilis encodes a bd-type terminal oxidase, cytochrome bc1 complex and several c-type cytochromes, yet lacks sequences homologous to any of the known bacterial cytochrome c oxidase genes. Recently, it was suggested that a putative respiratory cytochrome c peroxidase, receiving electrons from the cytochrome bc1 complex via cytochrome c552, ...
متن کاملGlycolytic enzymes in Zymomonas mobilis.
Raps, Shirley (University of Illinois, Urbana) and R. D. DeMoss. Glycolytic enzymes in Zymomonas mobilis. J. Bacteriol. 84:115-118. 1962-An enzyme extract of Zymomonas mobilis (Pseudomonas lindneri) was capable of fermenting glucose-6-phosphate to CO(2) and ethanol. The extract was found to contain phosphohexoisomerase, aldolase, and glyceraldehyde-3-phosphate dehydrogenase, but no demonstrable...
متن کاملRespiratory chain analysis of high ethanol producing Zymomonas mobilis mutants
Respiratory chain analysis of high ethanol producing Zymomonas mobilis mutants. 1 2 Takeshi Hayashi* Tsuyoshi Kato, and Kensuke Furukawa 3 4 Department of Food and Fermentation Science, Faculty of Food and Nutrition, Beppu 5 University, Beppu, Oita 874-8501, Japan 6 Food Science and Nutrition, Graduate School of Food Science and Nutrition, Beppu 7 University, Beppu, Oita 874-8501, Japan 8 9 *Co...
متن کاملPyruvate decarboxylase from Zymomonas mobilis
To study the mechanism of re-activation of Zymomonas mobilis pyruvate decarboxylase apoenzyme by its cofactors thiamin diphosphate and Mg2", cofactor-free enzyme was prepared by dialysis against I mM-dipicolinic acid at pH 8.2. This apoenzyme was then used in a series of experiments that included determination of: (a) the affinity towards one cofactor when the other was present at saturating co...
متن کاملProduction of Acetaldehyde by Zymomonas mobilis.
Mutants of Zymomonas mobilis were selected for decreased alcohol dehydrogenase activity by using consecutively higher concentrations of allyl alcohol. A mutant selected by using 100 mM allyl alcohol produced acetaldehyde at a level of 4.08 g/liter when the organism was grown in aerated batch cultures on a medium containing 4.0% (wt/wt) glucose. On the basis of the amount of glucose utilized, th...
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ژورنال
عنوان ژورنال: FEMS Microbiology Letters
سال: 1996
ISSN: 0378-1097,1574-6968
DOI: 10.1111/j.1574-6968.1996.tb08478.x