Transport of H+, K+, Na+ and Ca++ in Streptococcus

Heefner, D L

doi:10.1007/bf00226893

Cited by 49 publications

(23 citation statements)

References 256 publications

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“…The mechanism for the generation of the OH-radicals upon solar simulated light irradiation of TiON/TiO 2 leading to bacterial inactivation is suggested below in agreement with accepted knowledge in this area (Mills et al, 2012;Rtimi et al, 2012a;Subramanian et al, 2011;Ollis and Ekabi, 1993;Heefner, 1982) TiO …”

Section: Drs Tem and Afm Of The Tion Samplessupporting

confidence: 79%

Evidence for TiON sputtered surfaces showing accelerated antibacterial activity under simulated solar irradiation

2013

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New evidence is reported for TiON sputtered polyester surfaces activated by sunlight irradiation leading to the accelerated bacterial inactivation in the minute range. The absorption in Kubelka-Munk units of the TiON film was observed to be directly proportional to the time of Escherichia coli inactivation as detected by diffuse reflection spectroscopy (DRS). TiON layers were characterized by electron microscopy and by high angle angular dark field (HAADF) showing the continuous coverage of the polyester fibers by the TiON film. Ti 4+ /Ti 3+ redox catalysis was detected on the TiON surface by the XPS shifts during the bacteria inactivation process. Production of HO radicals on TiON-polyester as a function of sunlight irradiation was determined following the fluorescence of 2-hydroxyterephthalic acid. Release of Na and K-ions was determined by ICP-MS and provides the evidence that cell wall damage is a preceding step leading the bacterial inactivation. A stable performance of the TiON films was observed during repetitive bacterial inactivation.

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Section: Drs Tem and Afm Of The Tion Samplessupporting

confidence: 79%

Evidence for TiON sputtered surfaces showing accelerated antibacterial activity under simulated solar irradiation

2013

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“…On the basis of the TEM investigation, after treatment with the catalysts, the cell wall and cell membrane would be destroyed, subsequently leading to a change in cell membrane permeability and leakage of intracellular substances. K + exists universally in bacteria [24][25][26], and plays an important role in the regulation of polysome content and protein synthesis. Therefore, K + leakage from E. coli was used in this work to further examine the permeability of the cell membrane.…”

Section: Bactericidal Activity Of Silver Loaded Alumina On E Colimentioning

confidence: 99%

Efficient disinfection of Escherichia coli in water by silver loaded alumina

Qing-yun

2008

Journal of Inorganic Biochemistry

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a b s t r a c tThe catalytic inactivation of Escherichia coli (E. coli) in water by silver loaded alumina as catalyst was investigated. Ag/Al 2 O 3 and AgCl/Al 2 O 3 catalysts exhibited high bactericidal activity at room temperature in water with no need for any light or electrical power input. Dissolved oxygen which can be catalyzed to reactive oxygen species (ROS) was found to be essential for the strong bactericidal activities of the catalysts. Decomposition of the cell wall leading to leakage of the intracellular component and the complete lysis of the whole cell were directly observed by transmission electron microscopy (TEM). The resultant change in cell permeability was confirmed by potassium ion leakage. The different morphological changes between E. coli cells treated with the catalysts and Ag + were also observed. The formation of ROS involved in the bactericidal process by AgCl/Al 2 O 3 was confirmed by addition of catalase and Å OH scavenger. Higher temperature and pH value were found to have positive effect on the bactericidal activity of AgCl/Al 2 O 3 . All these results indicated that the bactericidal effect of the catalyst was a synergic action of ROS and Ag + , not an additive one. A possible mechanism is proposed.

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“…This is the first report indicating the existence of V(A) type ATPase in enterobacteria; here it is Na+-transporting ATPase but not H÷-ATPase. It is well known that E. hirae retains FoF; H÷-ATPase which extrudes protons and generates the proton potential [19]. Thus, two types of large multimeric ATPases are simultaneously expressed in this organism; F-type H+-ATPase functioning at low pH and V-type Na*-ATPase at high pH [2].…”

Section: Resultsmentioning

confidence: 99%

Primary structure of the α‐subunit of vacuolar‐type Na⁺‐ATPase inEnterococcus hirae Amplification of a 1000‐bp fragment by polymerase chain reaction

1991

FEBS Letters

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A 1000-bp fragment of Enteroeoccus hirae genomic DNA was amplified by the polymerase chain reaction method, using the oligonucleotide primers designed from amino acid sequences of both amino-terminal and a tryptic fragment of the Na*-ATPase ~-subunit in this organism. DNA sequencing of this product revealed that the amino acid sequence of Na÷-ATPase a-subunit is highly homologous to the corresponding sequences of large (~) subunits of vacuolar (archaebaeterial) type H*-ATPases. supporting our proposal [Kakinuma. Y. and Igarashi. K, (1990) FEBS Lett. 271.97-101] that the Na'-ATPase of this organism belongs to the vacuolar-type ATPase.

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Transport of H+, K+, Na+ and Ca++ in Streptococcus

Cited by 49 publications

References 256 publications

Evidence for TiON sputtered surfaces showing accelerated antibacterial activity under simulated solar irradiation

Evidence for TiON sputtered surfaces showing accelerated antibacterial activity under simulated solar irradiation

Efficient disinfection of Escherichia coli in water by silver loaded alumina

Primary structure of the α‐subunit of vacuolar‐type Na⁺‐ATPase inEnterococcus hirae Amplification of a 1000‐bp fragment by polymerase chain reaction

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Transport of H+, K+, Na+ and Ca++ in Streptococcus

Cited by 49 publications

References 256 publications

Evidence for TiON sputtered surfaces showing accelerated antibacterial activity under simulated solar irradiation

Evidence for TiON sputtered surfaces showing accelerated antibacterial activity under simulated solar irradiation

Efficient disinfection of Escherichia coli in water by silver loaded alumina

Primary structure of the α&#x2010;subunit of vacuolar&#x2010;type Na+&#x2010;ATPase inEnterococcus hirae Amplification of a 1000&#x2010;bp fragment by polymerase chain reaction

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Primary structure of the α‐subunit of vacuolar‐type Na⁺‐ATPase inEnterococcus hirae Amplification of a 1000‐bp fragment by polymerase chain reaction