Abstract
Bacteria accumulate high amounts of potassium in the cytoplasm. For studying transport of K+ (with86Rb as a marker) in bacteria (Staphylococcus aureus 17810S), the cells were depleted of the internal K+ pool by a DNP treatment. Kinetics and energetics of86Rb transport was assayed with glucose as an exogenous energy source. It was shown that86Rb uptake proceededvia a low affinity K+ transport system with an apparent,K m of 2.3 mmol/L Rb+. Studies with the lipophilic cation TPP+ (tetraphenylphosphonium), the protonophore CCCP (carbonyl cyanide 3-chlorophenylhydrazone) and inhibitors (HQNO-2-heptyl-4-hydroxyquinoline N-oxide; iodoacetate) indicated that86Rb transport was driven by Δψ (membrane potential) generatedvia the respiratory chain. The effect of Cd2+ on86Rb transport was assayed with two energy donors—glucose andL-lactate. It was found that Cd2+ strongly inhibited Δψ-dependent86Kb transport energized by cadmium-sensitive glucose oxidation, but was not toxic when cadmium-insensitivel-lactate was used as an energy source. The mechanism of these differential, substrate-dependent effects of Cd2+ on86Rb transport is discussed.
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Tynecka, Z., Malm, A., Kosikowska, U. et al. Substrate-dependent cadmium toxicity affecting energy-linked K+/86Rb transport inStaphylococcus aureus . Folia Microbiol 43, 617–622 (1998). https://doi.org/10.1007/BF02816378
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DOI: https://doi.org/10.1007/BF02816378