Reduced nicotinamide adenine dinucleotide oxidation in Escherichia coli particles

1967 ◽  
Vol 119 ◽  
pp. 194-201 ◽  
Author(s):  
P.D. Bragg ◽  
Cynthia Hou
1963 ◽  
Vol 9 (4) ◽  
pp. 531-539 ◽  
Author(s):  
Donald P. Zarowny ◽  
B. D. Sanwal

A nitrite reductase specific for reduced nicotinamide adenine dinucleotide (NADH) was purified approximately 30-fold from Escherichia coli, strain K12. The enzyme was metal sensitive, being inhibited by certain chelating agents and stimulated by others. The optimum pH for enzymic activity was 7.8–8.0 and the Michaelis constants for nitrite and NADH were 4.0 × 10−5 moles/l, and 3.3 × 10−4 moles/l., respectively. The partially purified enzyme did not show a flavin requirement and ammonia was not the product of the enzymic reaction.


Sign in / Sign up

Export Citation Format

Share Document