caa a22 4500 475746481 CHVBK 20180406123514.0 cr unu---uuuuu 170329e20001201xx s 000 0 eng 10.1007/s002840010155 doi (NATIONALLICENCE)springer-10.1007/s002840010155 Peroxide Reductase Activity of NADH Dehydrogenase in the Presence of an Endogenous 20-kDa Component of an Alkaliphilic Bacillus [Elektronische Daten] [Tsutomu Koitabashi, Takashi Satoh, Noriyuki Koyama] The membrane-bound NADH dehydrogenase of an alkaliphilic Bacillus YN-1 involved in the respiratory chain exhibits reductase activity for hydrogen peroxide and cumene hydroperoxide in the presence of the 22-kDa component (AhpC) from Amphibacillus xylanus (Koyama et al. Biochem. Biophys. Res. Commun. 247, 659-662). In this study, AhpC-like polypeptide with an apparent molecular mass of 20 kDa was isolated from the cell-free extract of YN-1. The NADH dehydrogenase exhibited reductase activity for cumene hydroperoxide in the presence of the purified AhpC-like component from YN-1. It is likely that the NADH dehydrogenase is not only involved in the respiratory chain, but also functions for scavenging peroxide in the presence of its own endogenous AhpC component. The enzyme expressed in Escherichia coli as a fusion protein with glutathione S-transferase (GST) showed the NADH dehydrogenase activity as high as the native enzyme from YN-1. While the fusion protein was unable to reduce cumene hydroperoxide in the presence of AhpC-like protein from YN-1, the protein obtained by the cleavage treatment of the fusion protein to release GST exhibited the reductase activity as much as the native enzyme. Springer-Verlag New York Inc., 2000 Koitabashi Tsutomu Department of Chemistry, Faculty of Science, Chiba University, Yayoi, Chiba 263-8522, Japan, Japan aut Satoh Takashi Department of Chemistry, Faculty of Science, Chiba University, Yayoi, Chiba 263-8522, Japan, Japan aut Koyama Noriyuki Department of Chemistry, Faculty of Science, Chiba University, Yayoi, Chiba 263-8522, Japan, Japan aut Current Microbiology Springer-Verlag 41/6(2000-12-01), 388-391 0343-8651 41:6<388 2000 41 284 https://doi.org/10.1007/s002840010155 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s002840010155 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Koitabashi Tsutomu Department of Chemistry, Faculty of Science, Chiba University, Yayoi, Chiba 263-8522, Japan, Japan aut NATIONALLICENCE 700 1- Satoh Takashi Department of Chemistry, Faculty of Science, Chiba University, Yayoi, Chiba 263-8522, Japan, Japan aut NATIONALLICENCE 700 1- Koyama Noriyuki Department of Chemistry, Faculty of Science, Chiba University, Yayoi, Chiba 263-8522, Japan, Japan aut NATIONALLICENCE 773 0- Current Microbiology Springer-Verlag 41/6(2000-12-01), 388-391 0343-8651 41:6<388 2000 41 284 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer