ISSN:
1432-0614
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
Summary From a thermophilic bacillus a viologen dependent pyridine nucleotide oxidoreductase has been purified and partially characterized. Its apparent molecular weight is about 120000 consisting of two subunits of equal or very similar molecular weight. Per molecular weight of 120000 the enzyme contains 4 FAD. FMN or labile sulfur could not be detected. The physiological role of the enzyme is not clear. It reduces NAD as well as NADP at the expense of reduced methylviologen. The reduced pyridine nucleotides can be reoxidized with carbamoylmethylviologen. The seven determined K m- and six K i-values show that the enzyme is suitable for the regeneration of NADH, NADPH, NAD and NADP. The stability in presence of oxidized and reduced methylviologen at 35°C or 60°C is satisfying for preparative work.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00286321
