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NADH dehydrogenase is the primary target for the bactericidal effect of CORM-2 in Shewanella oneidensis.
- Source :
-
Process Biochemistry . Nov2023:Part 1, Vol. 134, p22-31. 10p. - Publication Year :
- 2023
-
Abstract
- Shewanella oneidensis is a good model for investigating the bactericidal effects of chemical agents. In this study, the effects of tricarbonyldichlororuthenium dimer (CORM-2) on the aerobic and anaerobic growth of S. oneidensis were studied, and its bactericidal mechanisms were elucidated. CORM-2 (5 µM) significantly inhibited aerobic and anaerobic respiration. Growth potential tests showed that mutants Δ katB , Δ oxyR, Δ ccmF, and Δ crp and mutants that deleted each cytochrome c-encoding gene exhibited sensitivity to CORM-2 similar to that of the wild-type strain MR-1. Enzymatic analyses showed that cytochrome oxidase, catalase and cysteine desulfurase were activated by CORM-2, while nitrite reductase, nitrate reductase, sulfite reductase, thiosulfate reductase, peroxidase and NADH dehydrogenase were inhibited by CORM-2, and no significant changes were found in the activities of superoxide dismutase and aconitase. Promoter activity assays showed that cco , cyd , cox , katB , sirA and psrA were repressed by CORM-2. Sulfide alleviated the bactericidal effect of CORM-2 and protected NADH dehydrogenase from CORM-2 inhibition. Thus, oxidative stress and cytochrome oxidase inactivation are not the primary reasons for the bactericidal effect of CORM-2, and NADH dehydrogenase is the main target in S. oneidensis. The bactericidal effect of CORM-2 is caused by the toxicity of Ru2+, not by carbon monoxide. [Display omitted] • The first paper to investigate the effect of CORM-2 on the growth of S. oneidensis. • Cytochrome oxidase, catalase and cysteine desulfurase are activated by CORM-2. • Oxidative stress is not the major bactericidal reason of CORM-2 in S. oneidensis. • NADH dehydrogenase is the main target of CORM-2 in S. oneidensis. • The bactericidal effect of CORM-2 is caused by Ru2+, not by CO. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 13595113
- Volume :
- 134
- Database :
- Academic Search Index
- Journal :
- Process Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 173631136
- Full Text :
- https://doi.org/10.1016/j.procbio.2023.09.014