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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 161 (1994), S. 495-500 
    ISSN: 1432-072X
    Keywords: F1F0 ATPase ; Expression of unc genes ; Complementation analysis ; Membrane
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The aim of the present study was to construct functional hybrid ATPases consisting of all Escherichia coli ATPase subunits excepts the F0 subunits a or c which were replaced by the respective subunits of the Propionigenium modestum ATPase. This would give valuable information on the subunit(s) conferring the coupling ion specificity. Plasmids were constructed that carried the gene for subunit c (uncE) or subunit a (uncB) behind a tac promoter. These plasmids were transformed into E. coli strains which differed with respect to the unc operon and the expression of the P. modestum genes was verified biochemically. Enhanced expression of the P. modestum genes led to strong growth inhibition of all E. coli strains tested. However, the expressed P. modestum proteins could not functionally complement E. coli strains that lacked the homologous subunit.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 170 (1998), S. 69-77 
    ISSN: 1432-072X
    Keywords: Key words ATP synthase ; Decarboxylation ; Electrogenic substrate/product antiporter ; Sodium ion ; pump ; Malo-lactic fermentation ; Oxalate ; Malonate ; Succinate ; Glutarate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Decarboxylation of dicarboxylic acids (oxalate, malonate, succinate, glutarate, and malate) can serve as the sole energy source for the growth of fermenting bacteria. Since the free energy change of a decarboxylation reaction is small (around –20 kJ per mol) and equivalent to only approximately one-third of the energy required for ATP synthesis from ADP and phosphate under physiological conditions, the decarboxylation energy cannot be conserved by substrate-level phosphorylation. It is either converted (in malonate, succinate, and glutarate fermentation) by membrane-bound primary decarboxylase sodium ion pumps into an electrochemical gradient of sodium ions across the membrane; or, alternatively, an electrochemical proton gradient can be established by the combined action of a soluble decarboxylase with a dicarboxylate/monocarboxylate antiporter (in oxalate and malate fermentation). The thus generated electrochemical Na+ or H+ gradients are then exploited for ATP synthesis by Na+- or H+-coupled F1F0 ATP synthases. This new type of energy conservation has been termed decarboxylation phosphorylation and is responsible entirely for ATP synthesis in several anaerobic bacteria.
    Type of Medium: Electronic Resource
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