Journal
MICROBIOLOGY-SGM
Volume 155, Issue -, Pages 16-24Publisher
MICROBIOLOGY SOC
DOI: 10.1099/mic.0.022756-0
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Funding
- NIH [GM040388]
- Graduiertenforderung of the Federal State of Mecklenburg-Vorpommern
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM040388] Funding Source: NIH RePORTER
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An unusual non-haem chiron protein, reverse rubrerythrin (revRbr), is known to be massively upregulated in response to oxidative stress in the strictly anaerobic bacterium Clostridium acetobutylicum. In the present study both in vivo and in vitro results demonstrate an H2O2 and O-2 detoxification pathway in C. acetobutylicum involving revRbr, rubredoxin (Rd) and NADH: rubredoxin oxidoreductase (NROR). RevRbr exhibited both NADH peroxidase (NADH : H2O2 oxidoreductase) and NADH oxidase (NADH : O-2 oxidoreductase) activities in in vitro assays using NROR as the electron-transfer intermediary from NADH to revRbr. Rd increased the NADH consumption rate by serving as an intermediary electron-transfer shuttle between NROR and revRbr. While H2O2 was found to be the preferred substrate for revRbr, its relative oxidase activity was found to be significantly higher than that reported for other Rbrs, A revRbr-overexpressing strain of C. acetobutylicum showed significantly increased tolerance to H2O2 and O-2 exposure. RevRbr thus appears to protect C. acetobutylicum against oxidative stress by functioning as the terminal component of an NADH peroxidase and NADH oxidase.
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