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.
|Number of pages||5|
|Journal||Biochemical and Biophysical Research Communications|
|Publication status||Published - 2007 Oct 19|
Bibliographical noteFunding Information:
This work was supported by a research grant (KRF-2003-C00114) from the Korea Research Foundation. This work was also supported in part by Seoul R&BD Program and a Grant (KRF-2006-005-J04501) from Korea Research Foundation.
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology