Literature DB >> 354514

Cofactor role of iodide in peroxidase antimicrobial action against Escherichia coli.

E L Thomas, T M Aune.   

Abstract

The mechanism of antimicrobial activity of the peroxidase-hydrogen peroxide (H(2)O(2))-iodide (I(-)) system was investigated. Inhibition of respiration and loss of viability of Escherichia coli were used as measures of antimicrobial activity. Because the bacteria destroyed H(2)O(2), peroxidase antimicrobial action depended on the competition for H(2)O(2) between the bacteria and the peroxidase. Utilization of H(2)O(2) by the peroxidase was favored by (i) increasing either the peroxidase or the I(-) concentration, so as to increase the rate of oxidation of I(-), (ii) lowering the temperature to lower the rate of destruction of H(2)O(2) by the bacteria, and (iii) adding H(2)O(2) in small increments so as to avoid a large excess of H(2)O(2) relative to I(-). When utilization of H(2)O(2) by the peroxidase system was favored, the peroxidase system and iodine (I(2)) were equivalent. That is, antimicrobial action per mole of H(2)O(2) equaled that per mole of I(2). Also, identical antimicrobial action was obtained either by incubating the bacteria directly with the peroxidase system or by preincubating the peroxidase system so as to form I(2) and then adding the bacteria. On the other hand, peroxidase antimicrobial action could be obtained at low I(-) concentrations. These I(-) concentrations were lower than the concentration of I(2) that was required for antimicrobial action. It is proposed that peroxidase-catalyzed oxidation of I(-) yields I(2), which reacts with bacterial components to yield the oxidized components and I(-). The I(-) that is released can be reoxidized and participate again in the oxidation of bacterial components. In this way, I(-) acts as a cofactor in the peroxidase-catalyzed oxidation of bacterial components.

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Year:  1978        PMID: 354514      PMCID: PMC352380          DOI: 10.1128/AAC.13.6.1000

Source DB:  PubMed          Journal:  Antimicrob Agents Chemother        ISSN: 0066-4804            Impact factor:   5.191


  15 in total

1.  LACTOPEROXIDASE. II. ISOLATION.

Authors:  M MORRISON; D E HULTQUIST
Journal:  J Biol Chem       Date:  1963-08       Impact factor: 5.157

2.  Studies on the antibacterial action of human saliva. III. Cofactor requirements of Lactobacillus bactericidin.

Authors:  B J ZELDOW
Journal:  J Immunol       Date:  1963-01       Impact factor: 5.422

3.  Mutants of Escherichia coli requiring methionine or vitamin B12.

Authors:  B D DAVIS; E S MINGIOLI
Journal:  J Bacteriol       Date:  1950-07       Impact factor: 3.490

4.  Oxidation of protein sulfhydryls by products of peroxidase-catalyzed oxidation of thiocyanate ion.

Authors:  T M Aune; E L Thomas
Journal:  Biochemistry       Date:  1978-03-21       Impact factor: 3.162

5.  Peroxidase-catalyzed oxidation of protein sulfhydryls mediated by iodine.

Authors:  E L Thomas; T M Aune
Journal:  Biochemistry       Date:  1977-08-09       Impact factor: 3.162

6.  Lactoperoxidase-catalyzed incorporation of thiocyanate ion into a protein substrate.

Authors:  T M Aune; E L Thomas; M Morrison
Journal:  Biochemistry       Date:  1977-10-18       Impact factor: 3.162

7.  Hypothiocyanite ion; the inhibitor formed by the system lactoperoxidase-thiocyanate-hydrogen peroxide. I. Identification of the inhibiting compound.

Authors:  H Hoogendoorn; J P Piessens; W Scholtes; L A Stoddard
Journal:  Caries Res       Date:  1977       Impact factor: 4.056

8.  Susceptibility of Escherichia coli to bactericidal action of lactoperoxidase, peroxide, and iodide or thiocyanate.

Authors:  E L Thomas; T M Aune
Journal:  Antimicrob Agents Chemother       Date:  1978-02       Impact factor: 5.191

9.  Accumulation of hypothiocyanite ion during peroxidase-catalyzed oxidation of thiocyanate ion.

Authors:  T M Aune; E L Thomas
Journal:  Eur J Biochem       Date:  1977-10-17

10.  Studies on the chlorinating activity of myeloperoxidase.

Authors:  J E Harrison; J Schultz
Journal:  J Biol Chem       Date:  1976-03-10       Impact factor: 5.157

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  6 in total

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

Authors:  E L Thomas
Journal:  Infect Immun       Date:  1979-02       Impact factor: 3.441

2.  Effect of growth phase and cell envelope structure on susceptibility of Salmonella typhimurium to the lactoperoxidase-thiocyanate-hydrogen peroxide system.

Authors:  M A Purdy; J Tenovuo; K M Pruitt; W E White
Journal:  Infect Immun       Date:  1983-03       Impact factor: 3.441

3.  Myeloperoxidase-hydrogen peroxide-chloride antimicrobial system: effect of exogenous amines on antibacterial action against Escherichia coli.

Authors:  E L Thomas
Journal:  Infect Immun       Date:  1979-07       Impact factor: 3.441

4.  Hemoglobins Likely Function as Peroxidase in Blood Clam Tegillarca granosa Hemocytes.

Authors:  Sufang Wang; Xiaopei Yu; Zhihua Lin; Shunqin Zhang; Liangyi Xue; Qinggang Xue; Yongbo Bao
Journal:  J Immunol Res       Date:  2017-01-15       Impact factor: 4.818

5.  The iron-H2O2-iodide cytotoxic system.

Authors:  S J Klebanoff
Journal:  J Exp Med       Date:  1982-10-01       Impact factor: 14.307

Review 6.  Mode of action of lactoperoxidase as related to its antimicrobial activity: a review.

Authors:  F Bafort; O Parisi; J-P Perraudin; M H Jijakli
Journal:  Enzyme Res       Date:  2014-09-16
  6 in total

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