Open AccessNADH dehydrogenase of Corynebacterium glutamicum . Purification of an NADH dehydrogenase II homolog able to oxidize NADPH
Author(s) -
Matsushita Kazunobu,
Otofuji Asuka,
Iwahashi Midori,
Toyama Hirohide,
Adachi Osao
Publication year - 2001
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2001.tb10896.x
Subject(s) - corynebacterium glutamicum , biochemistry , dehydrogenase , nadh dehydrogenase , chemistry , enzyme , nad+ kinase , biology , gene , protein subunit
NADPH oxidase activity, in addition to NADH oxidase activity, has been shown to be present in the respiratory chain of Corynebacterium glutamicum . In this study, we tried to purify NADPH oxidase and NADH dehydrogenase activities from the membranes of C. glutamicum . Both the enzyme activities were simultaneously purified in the same fraction, and the purified enzyme was shown to be a single polypeptide of 55 kDa. The N‐terminal sequence of the enzyme was consistent with the sequence deduced from the NADH dehydrogenase gene of C. glutamicum , which has been sequenced and shown to be a homolog of NADH dehydrogenase II. In addition to high NADH–ubiquinone‐1 oxidoreductase activity at neutral pH, the purified enzyme showed relatively high NADPH oxidase and NADPH–ubiquinone‐1 oxidoreductase activities at acidic pH. Thus, NADH dehydrogenase of C. glutamicum was shown to be rather unique in having a relatively high reactivity toward NADPH.