dc.contributor.authorWang, Liang
dc.contributor.authorChong, Huiqing
dc.contributor.authorJiang, Rongrong
dc.date.accessioned2013-07-31T06:20:45Z
dc.date.available2013-07-31T06:20:45Z
dc.date.copyright2012en_US
dc.date.issued2012
dc.identifier.citationWang, L., Chong, H.,& Jiang, R. (2012). Comparison of alkyl hydroperoxide reductase and two water-forming NADH oxidases from Bacillus cereus ATCC 14579. Applied Microbiology and Biotechnology, 96(5), 1265-1273.en_US
dc.identifier.urihttp://hdl.handle.net/10220/12616
dc.description.abstractBacillus cereus (B. cereus) is an ubiquitous facultative anaerobic bacterium, and its growth in aerobic environment correlates to the functions of its oxygen defense system. Water-forming NADH oxidase (nox-2) can catalyze the conversion of oxygen to water with concomitant NADH oxidation in anaerobic microorganisms. Here, we report the cloning and characterization of two annotated nox-2 s (nox-2(444) and nox-2(554)) from B. cereus ATCC 14579 and their comparison with another oxidative stress defense system alkyl hydroperoxide reductase (AhpR) from this microbe, which composed of two enzymes—hydrogen peroxide-forming NADH oxidase (nox-1) and peroxidase. Both nox-2 and AhpR catalyze the same reaction in the presence of oxygen. With the stimulation of exogenously added FAD, the maximum activity of nox-1, nox-2(444), and nox-2(554) could reach 27.7 U/mg, 22.9 U/mg, and 2.4 U/mg, respectively, at pH 7.0, 30 °C. Different from nox-1, both nox-2 s were thermotolerant enzymes and could maintain above 87% of their optimum activity at 80 °C, which was not found in other nox-2 s. As for operational stability, all are turnover-limited. Exogenously added reductive reagent dithiothreitol could dramatically increase the total turnover number of nox-2(444) and nox-2(554) by twofold and threefold, respectively, but had no effect on AhpR or nox-1.en_US
dc.language.isoenen_US
dc.relation.ispartofseriesApplied microbiology and biotechnologyen_US
dc.titleComparison of alkyl hydroperoxide reductase and two water-forming NADH oxidases from Bacillus cereus ATCC 14579en_US
dc.typeJournal Article
dc.contributor.schoolSchool of Chemical and Biomedical Engineeringen_US
dc.identifier.doihttp://dx.doi.org/10.1007/s00253-012-3919-1


Files in this item

FilesSizeFormatView

There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record