Peroxide reductase activity of NADH dehydrogenase of an alkaliphilic Bacillus in the presence of a 22-kDa protein component from Amphibacillus xylanus

Biochemical and Biophysical Research Communications
N KoyamaV Massey

Abstract

The NADH oxidase of Amphibacillus xylanus shows high NADH-peroxide reductase activity for hydrogen peroxide and alkyl hydroperoxides in the presence of a 22-kDa disulfide-containing protein component (Y. Niimura, L. B. Poole, and V. Massey, J. Biol.Chem. 270, 25645-25650, 1995). It was found that the membrane-bound NADH dehydrogenase of an alkaliphilic Bacillus (YN-1) involved in the respiratory chain also exhibits reductase activity for hydrogen peroxide and cumene hydroperoxide in the presence of the 22-kDa component from Amphibacillus xylanus. Vmax values for these substrates were as high as those of the NADH oxidase of A. xylanus. Although the 38-kDa protein produced by trypsin treatment of NADH dehydrogenase retains NADH dehydrogenase activity, it exhibited no peroxide reductase activity in the presence of the 22-kDa component from A. xylanus. The NADH dehydrogenase of YN-1 might not only catalyze electron flow from NADH to the respiratory chain, but also function for scavenging peroxide.

References

Feb 1, 1975·Journal of General Microbiology·K OtaY Noso
Apr 1, 1989·Journal of Biochemistry·X M XuK Tsuda
Jul 31, 1980·Biochemical and Biophysical Research Communications·R J LewisT A Krulwich
Nov 29, 1996·The Journal of Biological Chemistry·Y Niimura, V Massey

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Citations

Sep 30, 2000·European Journal of Biochemistry·L B PooleM Li Calzi
Jun 1, 2010·International Migration·Douglas S MasseyDirgha J Ghimire
Feb 3, 2000·Free Radical Biology & Medicine·L B PooleY Kamio

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