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Studies on the regulation of assimilatory nitrate reductase in Ankistrodesmus braunii

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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

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Authors and Affiliations

  1. Departamento de Bioquímica, Facultad de Ciencias y CSIC, Universidad de Sevilla, Sevilla, Spain

    J. Diez, A. Chaparro, J. M. Vega & A. Relimpio

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  1. J. Diez
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  2. A. Chaparro
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  3. J. M. Vega
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  4. A. Relimpio
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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

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