Abstract
In the green alga Ankistrodesmus braunii, all the activities associated with the nitrate reductase complex (i.e., NAD(P)H-nitrate reductase, NAD(P)H-cytochrome c reductase and FMNH2-or MVH-nitrate reductase) are nutritionally repressed by ammonia or methylamine. Besides, ammonia or methylamine promote in vivo the reversible inactivation of nitrate reductase, but not of NAD(P)H-cytochrome c reductase. Subsequent removal of the inactivating agent from the medium causes reactivation of the inactive enzyme. Menadione has a striking stimulation on the in vivo reactivation of the inactive enzyme. The nitrate reductase activities, but not the diaphorase activity, can be inactivated in vitro by preincubating a partially purified enzyme preparation with NADH or NADPH. ADP, in the presence of Mg2+, presents a cooperative effect with NADH in the in vitro inactivation of nitrate reductase. This effect appears to be maximum at a concentration of ADP equimolecular with that of NADH.
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Abbreviations
- ADP:
-
Adenosine-5′-diphosphate
- AMP:
-
Adenosine-5′-monophosphate
- ATP:
-
Adenosine-5′-triphosphate
- FAD:
-
Flavin adenine dinucleotide
- FMNH2 :
-
Flavin adenine mononucleotide, reduced form
- GDP:
-
Guanosine-5′-diphosphate
- MVH:
-
Methyl viologen, reduced form
- NADH:
-
Nicotinamide adenine dinucleotide, reduced form
- NADPH:
-
Nicotinamide adenine dinucleotide phosphate, reduced form
References
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Diez, J., Chaparro, A., Vega, J.M. et al. Studies on the regulation of assimilatory nitrate reductase in Ankistrodesmus braunii . Planta 137, 231–234 (1977). https://doi.org/10.1007/BF00388155
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DOI: https://doi.org/10.1007/BF00388155