Oxidative inactivation of Escherichia coli by hypochlorous acid

@article{Albrich1982OxidativeIO,
  title={Oxidative inactivation of Escherichia coli by hypochlorous acid},
  author={J. Michael Albrich and Jeanette K. Hurst},
  journal={FEBS Letters},
  year={1982},
  volume={144}
}

Hypochlorous acid and myeloperoxidase-catalyzed oxidation of iron-sulfur clusters in bacterial respiratory dehydrogenases.

Loss of succinate-dependent respiration was closely associated with HOCl and myeloperoxidase-mediated microbicidal activity against P. aeruginosa and was also an early event in the oxidant-mediated metabolic dysfunctions of E. coli, but these effects were not caused by the destruction of the Fe/S clusters within the succinate:ubiquinone oxidoreductase.

Living with a Killer: The Effects of Hypochlorous Acid on Mammalian Cells

Recent reports have indicated that HOCl can activate cell signaling pathways, and these studies may provide important information on the role of this oxidant in inflammation.

General mechanism for the bacterial toxicity of hypochlorous acid: abolition of ATP production.

These results establish that cellular death is accompanied by complete disruption of bacterial ATP production by both oxidative and fermentative pathways as a consequence of inhibition of inner membrane bound systems responsible for these processes.

Leukocytic oxygen activation and microbicidal oxidative toxins.

Focus is placed on recent research on cidal mechanisms of HOCl, including the oxidative biochemistry of active chlorine compounds, identification of sites of lesions in bacteria, and attendant metabolic consequences.

Oxidative mechanisms utilized by human neutrophils to destroy Escherichia coli.

It is demonstrated that neutrophils have the potential to utilize the myeloperoxidase system to generate bactericidal quantities of a species with characteristics similar to, if not identical with, hypochlorous acid.

Oxidative mechanisms utilized by human neutrophils to destroy Escherichia coli

It is demonstrated that neutrophils have the potential to utilize the myeloperoxidase system to generate bactericidal quantities of a species with characteristics similar to, if not identical with, hypochlorous acid.

Differential Effects of Myeloperoxidase-Derived Oxidants on Escherichia coli DNA Replication

It is proposed that one of these requirements, common to oriC and the P1 origin but not critical to the replication of the other non-oriC plasmids, is an important target for MPO-mediated oxidations that mediate the initial decline in E. colichromosomal DNA synthesis.

Investigations on apocynin, a potent NADPH oxidase inhibitor

Experiments are described that have led to a better understanding of the mode of action by which apocynin inhibits the ROS production by activated human PMNs, and one of the conclusions is that apoynin itself is not active, but that it is converted into an active dimer inside the phagosomes of activated PMNs.
...

References

SHOWING 1-10 OF 22 REFERENCES

Biological reactivity of hypochlorous acid: implications for microbicidal mechanisms of leukocyte myeloperoxidase.

The reactivity patterns observed are consistent with the view that bactericidal action results primarily from loss of energy-linked respiration due to destruction of cellular electron transport chains and the adenine nucleotide pool.

Oxidative Peptide Cleavage and Decarboxylation by the MPO-H2O2-Cl− Antimicrobial System

It appears that myeloperoxidase (MPO) can not only decarboxylate free and bound amino acids, yielding aldehydes, but also it can actively participate in oxidative peptide cleavage, which may play a critical role in the microbicidal action of the leukocyte.

Myeloperoxidase, hydrogen peroxide, chloride antimicrobial system: nitrogen-chlorine derivatives of bacterial components in bactericidal action against Escherichia coli

  • E. Thomas
  • Chemistry, Biology
    Infection and immunity
  • 1979
The N-Cl derivatives could oxidize bacterial components long after the myeloperoxidase-catalyzed oxidation of chloride was complete, suggesting that peptides were fragmented by oxidative cleavage of chloramide derivatives of peptide bonds.

Myeloperoxidase-Hydrogen Peroxide-Chloride Antimicrobial System: Effect of Exogenous Amines on Antibacterial Action Against Escherichia coli

  • E. Thomas
  • Chemistry, Biology
    Infection and immunity
  • 1979
An important role for leukocyte amine components in myeloperoxidase-catalyzed antimicrobial activity in vivo is suggested, due to the ability of NH(2)Cl to penetrate the hydrophobic cell membrane and thus to oxidize intracellular components.

Role of the Phagocyte in Host-Parasite Interactions XXVII. Myeloperoxidase-H2O2-Cl−-Mediated Aldehyde Formation and Its Relationship to Antimicrobial Activity

Evidence is presented which suggests that the mechanism of action of the myeloperoxidase-H(2)O(2)-Cl(-) antimicrobial system in the phagocyte is by the formation of aldehydes, which appears to be different from that found with Cl(-).

Enhanced killing of myeloperoxidase-coated bacteria in the myeloperoxidase-H2O2-Cl- system.

Bacteria preincubated with myeloperoxidase (MPO) are more readily killed upon the addition of H2O2 and Cl- than controls not subject to prior incubation. This effect was evidenced by decreased

Oxygen metabolism and the toxic properties of phagocytes.

The products of oxygen reduction and excitation and enzymes that potentiate or limit the toxicity of these agents contribute to the complexity of the oxygen-dependent antimicrobial systems of phagocytes.

Effects of Phagocytosis by Rabbit Granulocytes on Macromolecular Synthesis and Degradation in Different Species of Bacteria

Evidence indicates that the E. coli envelope retains sufficient structural organization to preserve integrated biochemical function for at least 1 h after the bacteria have lost the ability to multiply.

Effect of the proton electrochemical gradient on maleimide inactivation of active transport in Escherichia coli membrane vesicles.

The findings are consistent with the notion that delta muH+, in addition to acting as the immediate driving force the active transport, may bring about structural or conformational changes in certain membrane proteins that catalyze active transport.