PMID:22081210
| Citation |
Trchounian, K, Pinske, C, Sawers, RG and Trchounian, A (2011) Dependence on the F0F1-ATP synthase for the activities of the hydrogen-oxidizing hydrogenases 1 and 2 during glucose and glycerol fermentation at high and low pH in Escherichia coli. J. Bioenerg. Biomembr. 43:645-50 |
|---|---|
| Abstract |
Escherichia coli has four [NiFe]-hydrogenases (Hyd); three of these, Hyd-1, Hyd-2 and Hyd-3 have been characterized well. In this study the requirement for the F(0)F(1)-ATP synthase for the activities of the hydrogen-oxidizing hydrogenases Hyd-1 and Hyd-2 was examined. During fermentative growth on glucose at pH 7.5 an E. coli F(0)F(1)-ATP synthase mutant (DK8) lacked hydrogenase activity. At pH 5.5 hydrogenase activity was only 20% that of the wild type. Using in-gel activity staining, it could be demonstrated that both Hyd-1 and Hyd-2 were essentially inactive at these pHs, indicating that the residual activity at pH 5.5 was due to the hydrogen-evolving Hyd-3 enzyme. During fermentative growth in the presence of glycerol, hydrogenase activity in the mutant was highest at pH 7.5 attaining a value of 0.76 U/mg, or ~50% of wild type activity, and Hyd-2 was only partially active at this pH, while Hyd-1 was inactive. Essentially no hydrogenase activity was measured at pH 5.5 during growth with glycerol. At this pH the mutant had a hydrogenase activity that was maximally only ~10% of wild type activity with either carbon substrate but a weak activity of both Hyd-1 and Hyd-2 could be detected. Taken together, these results demonstrate for the first time that the activity of the hydrogen-oxidizing hydrogenases in E. coli depends on an active F(0)F(1)-ATP synthase during growth at high and low pH. |
| Links |
PubMed Online version:10.1007/s10863-011-9397-9 |
| Keywords |
Cryoprotective Agents/metabolism; Cryoprotective Agents/pharmacology; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Fermentation/physiology; Glucose/metabolism; Glucose/pharmacology; Glycerol/metabolism; Glycerol/pharmacology; Hydrogen-Ion Concentration; Mutation; Oxidoreductases/genetics; Oxidoreductases/metabolism; Proton-Translocating ATPases/genetics; Proton-Translocating ATPases/metabolism; Sweetening Agents/metabolism; Sweetening Agents/pharmacology |
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