Carbon monoxide dehydrogenase in mycobacteria possesses a nitric oxide dehydrogenase activity. Academic Article uri icon

Overview

abstract

  • CO dehydrogenase (CO-DH) catalyzes the oxidation of CO to CO(2) 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.

publication date

  • August 10, 2007

Research

keywords

  • Aldehyde Oxidoreductases
  • Multienzyme Complexes
  • Mycobacterium
  • Nitric Oxide
  • Oxidoreductases

Identity

Scopus Document Identifier

  • 34548209875

Digital Object Identifier (DOI)

  • 10.1016/j.bbrc.2007.08.011

PubMed ID

  • 17707766

Additional Document Info

volume

  • 362

issue

  • 2