Carbon monoxide dehydrogenase in mycobacteria possesses a nitric oxide dehydrogenase activity

Sae Woong Park, Taeksun Song, Seo Young Kim, Eungbin KIm, Jeong Il Oh, Chi Yong Eom, Young Min Kim

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

CO dehydrogenase (CO-DH) catalyzes the oxidation of CO to CO2 in carboxydobacteria. Cell-free extracts prepared from several mycobacteria, including Mycobacterium tuberculosis H37Ra, showed NO dehydrogenase (NO-DH) activity in a reaction mixture containing sodium nitroprusside (SNP) as the source of NO. The association of the NO-DH activity with CO-DH was revealed by activity staining and confirmed by enzyme assay with purified CO-DH from Mycobacterium sp. strain JC1, a carboxydotrophic mycobacterium. SNP stimulated the production of CO-DH with a coincidental increase in NO-DH activity in the bacterium, further supporting this association and implying the existence of a possible SNP-induced CO-DH gene expression. The addition of purified CO-DH to cultures of Escherichia coli revealed that the enzyme protected E. coli from SNP-induced killing in a dose-dependant way. The present results indicate that mycobacterial CO-DH also acts as a NO-DH, which may function in the protection of mycobacterial pathogens from nitrosative stress during infection.

Original languageEnglish
Pages (from-to)449-453
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume362
Issue number2
DOIs
Publication statusPublished - 2007 Oct 19

Fingerprint

carbon monoxide dehydrogenase
Mycobacterium
Oxidoreductases
Nitric Oxide
Nitroprusside
Escherichia coli
Association reactions
Enzyme Assays
Pathogens
Enzymes
Carbon Monoxide
Cell Extracts
Mycobacterium tuberculosis
Gene expression
Assays
Bacteria

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Park, Sae Woong ; Song, Taeksun ; Kim, Seo Young ; KIm, Eungbin ; Oh, Jeong Il ; Eom, Chi Yong ; Kim, Young Min. / Carbon monoxide dehydrogenase in mycobacteria possesses a nitric oxide dehydrogenase activity. In: Biochemical and Biophysical Research Communications. 2007 ; Vol. 362, No. 2. pp. 449-453.
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Carbon monoxide dehydrogenase in mycobacteria possesses a nitric oxide dehydrogenase activity. / Park, Sae Woong; Song, Taeksun; Kim, Seo Young; KIm, Eungbin; Oh, Jeong Il; Eom, Chi Yong; Kim, Young Min.

In: Biochemical and Biophysical Research Communications, Vol. 362, No. 2, 19.10.2007, p. 449-453.

Research output: Contribution to journalArticle

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AU - Park, Sae Woong

AU - Song, Taeksun

AU - Kim, Seo Young

AU - KIm, Eungbin

AU - Oh, Jeong Il

AU - Eom, Chi Yong

AU - Kim, Young Min

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N2 - CO dehydrogenase (CO-DH) catalyzes the oxidation of CO to CO2 in carboxydobacteria. Cell-free extracts prepared from several mycobacteria, including Mycobacterium tuberculosis H37Ra, showed NO dehydrogenase (NO-DH) activity in a reaction mixture containing sodium nitroprusside (SNP) as the source of NO. The association of the NO-DH activity with CO-DH was revealed by activity staining and confirmed by enzyme assay with purified CO-DH from Mycobacterium sp. strain JC1, a carboxydotrophic mycobacterium. SNP stimulated the production of CO-DH with a coincidental increase in NO-DH activity in the bacterium, further supporting this association and implying the existence of a possible SNP-induced CO-DH gene expression. The addition of purified CO-DH to cultures of Escherichia coli revealed that the enzyme protected E. coli from SNP-induced killing in a dose-dependant way. The present results indicate that mycobacterial CO-DH also acts as a NO-DH, which may function in the protection of mycobacterial pathogens from nitrosative stress during infection.

AB - CO dehydrogenase (CO-DH) catalyzes the oxidation of CO to CO2 in carboxydobacteria. Cell-free extracts prepared from several mycobacteria, including Mycobacterium tuberculosis H37Ra, showed NO dehydrogenase (NO-DH) activity in a reaction mixture containing sodium nitroprusside (SNP) as the source of NO. The association of the NO-DH activity with CO-DH was revealed by activity staining and confirmed by enzyme assay with purified CO-DH from Mycobacterium sp. strain JC1, a carboxydotrophic mycobacterium. SNP stimulated the production of CO-DH with a coincidental increase in NO-DH activity in the bacterium, further supporting this association and implying the existence of a possible SNP-induced CO-DH gene expression. The addition of purified CO-DH to cultures of Escherichia coli revealed that the enzyme protected E. coli from SNP-induced killing in a dose-dependant way. The present results indicate that mycobacterial CO-DH also acts as a NO-DH, which may function in the protection of mycobacterial pathogens from nitrosative stress during infection.

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