The study is designed to investigate bactericidal actions of electrolyzed oxidizing water on hospital infections. Ten of the most common opportunistic pathogens are used for this study. Cultures are inoculated in 4.5 mL of electrolyzed oxidizing (EO) water or 4.5 mL of sterile deionized water (control), and incubated for 0, 0.5, and 5 min at room temperature. At the exposure time of 30 s the EO water completely inactivates all of the bacterial strains, with the exception of vegetative cells and spores of bacilli which need 5 min to be killed. The results indicate that electrolyzed oxidizing water may be a useful disinfectant for hospital infections, but its clinical application has still to be evaluated.

The uncoupler-induced inactivation of H+-ATPase in hepatoma 22a and mouse liver mitochondria has been studied. The dependence of this process on d,uH, and pH and ATP was established. The inactivated ATPase could be reactivated at alkaline pH values in the absence of ATP. These data indicate that the inactivation is apparently caused by the natural protein inhibitor. ATP-and pH-dependent decrease of ATPase activity is also observed after Lubrol-WX disruption of mitochondria. It can be proposed that practically all ATPase molecules in hepatoma mitochondria are in a catalytically active complex with the protein inhibitor. At low dpH this complex is inactivated via reversible pH-dependent and irreversible ATP-dependent rearrangements. The pH-dependent rearrangement of the isolated protein inhibitor from hepatoma mitrochondria is also observed.

Almost all ATPase molecules in submitochondrial particles, isolated from beef heart mitochondria in the presence of MgATP, are in an inactive complex with the natural protein inhibitor (IF1). In de‐energized particles at high ionic strength a slow and irreversible ATPase activation is found to occur due to a dissociation of the enzyme‐inhibitor complex. The pH‐dependence of this process points out that deprotonation of IF1 molecule is an essential step in the dissociation of the complex. Zn2+ sharply accelerates ATPase activation, probably via binding with the deprotonated form of IF1. ATPase activation is completely prevented by MgATP, indicating the formation of a transient enzyme‐inhibitor complex retaining ATPase activity

Propionibacterium freudenreichii subsp. shermanii is known to prevent mutations caused by various agents such as N-methyl-N'-nitro-N-nitrosoguanidine, 9-aminoacridine, 4-nitro-quinoline-1-oxide and by UV radiation in both prokaryotic and eukaryotic cells. It was also shown to prevent or repair damage caused by H(2)O(2) or UV radiation in Salmonella typhimurium and Escherichia coli, a characteristic previously designated as reactivative effect. In order to characterise this effect at the molecular level, we have purified the active component from a P. freudenreichii cell-free extract using a combination of ammonium sulfate precipitation, anion-exchange and size-exclusion chromatography. The isolated 35 kDa protein was then identified using both N-terminal and internal peptide sequencing as a cysteine synthase. The latter was localised in the P. freudenreichii proteomic map. It is constitutively expressed but also clearly induced during adaptation to detergent and heat, but not acid, stresses. The biological meaning of cysteine synthase in the context of adaptation to oxidative and non-oxidative stresses is discussed.

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