Active and inactive nitrate reductase. Effects of mild treatment with denaturing agents of protein.
Nitrate reductase (NAD(P)H:nitrate oxidoreductase, EC 1.6.6.2) of the unicellular alga Cyanidium caldarium can exist in two interconvertible forms; one catalytically active and one inactive. The inactive nitrate reductase can be activated by mild treatment with denaturing agents of protein. By treatment with urea or mersalyl, activation of both the NADPH and benzyl viologen activities can be realized under mild conditions, whereas by treatment with heat, the activation of benzyl viologen activity is concomitant with loss of the NADPH activity. On the other hand, both activities are activated and destroyed concomitantly by ethylene glycol. In the present of FAD, either activation of benzyl viologen activity or loss of NADPH activity upon heating occur only at higher temperatures. The existence of a controlling region in the nitrate reductase molecule is postulated.
D001594:Benzyl Viologen / Q000378:metabolism; D004789:Enzyme Activation / Q000187:drug effects; D005026:Ethylene Glycols / Q000494:pharmacology; D005182:Flavin-Adenine Dinucleotide / Q000494:pharmacology; D006358:Hot Temperature; D008634:Mersalyl / Q000494:pharmacology; D009249:NADP / Q000378:metabolism; D009565:Nitrate Reductases / Q000378:metabolism*; D010944:Plants / Q000201:enzymology*; D011489:Protein Denaturation; D000461:Rhodophyta / Q000201:enzymology; D014508:Urea / Q000494:pharmacology
D005026:Ethylene Glycols; D001594:Benzyl Viologen; D005182:Flavin-Adenine Dinucleotide; D009249:NADP; D008634:Mersalyl; D014508:Urea; D009565:Nitrate Reductases