1887

Abstract

An unusual non-haem diiron protein, reverse rubrerythrin (revRbr), is known to be massively upregulated in response to oxidative stress in the strictly anaerobic bacterium . In the present study both and results demonstrate an HO and O detoxification pathway in involving revRbr, rubredoxin (Rd) and NADH : rubredoxin oxidoreductase (NROR). RevRbr exhibited both NADH peroxidase (NADH : HO oxidoreductase) and NADH oxidase (NADH : O oxidoreductase) activities in 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 HO 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 showed significantly increased tolerance to HO and O exposure. RevRbr thus appears to protect against oxidative stress by functioning as the terminal component of an NADH peroxidase and NADH oxidase.

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2009-01-01
2024-03-28
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