[NROR_CLOAB] Catalyzes the NADH-dependent reduction of rubredoxin (Rd). NADPH is a very poor electron donor compared to NADH. Functions as an intermediate component in the electron transfer chain: NADH->NROR->Rd->FprA1/2. Also functions as an intermediate component in the electron transfer chains from NADH to revRbr and Dfx. Therefore, is a key electron carrier in an efficient multienzyme complex that can scavenge O(2) and reactive oxygen species (ROS), and thus plays an important role in the oxidative stress defense system in C.acetobutylicum, an obligate anaerobic bacterium.[1][2][3][4]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
↑Guedon E, Petitdemange H. Identification of the gene encoding NADH-rubredoxin oxidoreductase in Clostridium acetobutylicum. Biochem Biophys Res Commun. 2001 Jul 13;285(2):496-502. PMID:11444870 doi:10.1006/bbrc.2001.5196
↑Hillmann F, Riebe O, Fischer RJ, Mot A, Caranto JD, Kurtz DM Jr, Bahl H. Reductive dioxygen scavenging by flavo-diiron proteins of Clostridium acetobutylicum. FEBS Lett. 2009 Jan 5;583(1):241-5. doi: 10.1016/j.febslet.2008.12.004. Epub 2008, Dec 11. PMID:19084524 doi:10.1016/j.febslet.2008.12.004
↑Riebe O, Fischer RJ, Wampler DA, Kurtz DM Jr, Bahl H. Pathway for H2O2 and O2 detoxification in Clostridium acetobutylicum. Microbiology. 2009 Jan;155(Pt 1):16-24. doi: 10.1099/mic.0.022756-0. PMID:19118342 doi:10.1099/mic.0.022756-0
↑Kawasaki S, Sakai Y, Takahashi T, Suzuki I, Niimura Y. O2 and reactive oxygen species detoxification complex, composed of O2-responsive NADH:rubredoxin oxidoreductase-flavoprotein A2-desulfoferrodoxin operon enzymes, rubperoxin, and rubredoxin, in Clostridium acetobutylicum. Appl Environ Microbiol. 2009 Feb;75(4):1021-9. doi: 10.1128/AEM.01425-08. Epub, 2009 Jan 5. PMID:19124587 doi:10.1128/AEM.01425-08
