Reactions of the Escherichia coli flavohaemoglobin (Hmp) with oxygen and reduced nicotinamide adenine dinucleotide: evidence for oxygen switching of flavin oxidoreduction and a mechanism for oxygen sensing

1994 ◽  
Vol 255 (1344) ◽  
pp. 251-258 ◽  
Keyword(s):  
Escherichia Coli ◽  
Nicotinamide Adenine Dinucleotide ◽  
Oxygen Sensing ◽  
Nicotinamide Adenine ◽  
Reduced Nicotinamide Adenine Dinucleotide

CHARACTERIZATION OF A NICOTINAMIDE ADENINE DINUCLEOTIDE SPECIFIC NITRITE REDUCTASE FROM ESCHERICHIA COLI, STRAIN K12

1963 ◽  
Vol 9 (4) ◽  
pp. 531-539 ◽  
Author(s):  
Donald P. Zarowny ◽  
B. D. Sanwal
Keyword(s):  
Escherichia Coli ◽  
Nitrite Reductase ◽  
Nicotinamide Adenine Dinucleotide ◽  
Enzymic Activity ◽  
Coli Strain ◽  
Nicotinamide Adenine ◽  
Optimum Ph ◽  
Michaelis Constants ◽  
Reduced Nicotinamide Adenine Dinucleotide

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.

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