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Purification and properties of a nitrite reductase ec 1.7.7.1 from porphyra yezoensis



Purification and properties of a nitrite reductase ec 1.7.7.1 from porphyra yezoensis



Plant and Cell Physiology 17(3): 417-430



Nitrite reductase was extracted from the red alga P. yezoensis Ueda and purified through precipitation with ammonium sulfate, column chromatographies and polyacrylamide gel disc electrophoresis. The enzyme preparation thus obtained showed a single band on disc electrophoresis. The absorption spectrum had 3 maxima at 385 nm (Soret band), 580 nm (.alpha.-band), and 278 nm; the ratio of absorbance of the Soret band to the .alpha.-band was 4.3. The MW and the number of amino acid residues were estimated to be 63,000 and 601, respectively. The enzyme activity was optimal at around pH 7.5, and its activity was heat labile as indicated by reduction of activity by about 70% when heated at 37.degree. C for 10 min. The enzyme used ferredoxin and methyl viologen, but not NADP+ or NAD+, as the electron carriers. Moreover, reduced forms of the latter two showed no effect on its activity. Km values of this enzyme for NO2-, Fd [ferredoxin] and MV [methyl viologen] were 8.1 .times. 104 M, 4.3 .times. 10-8 M, and 3.7 .times. 10-4 M, respectively. Almost half of its activity was lost when potassium cyanide was added at a concentration as low as 10-5 M, and the Ki value was 1.8 .times. 10-5 M. Thus, the nitrite reductase of Porphyra must be systematically grouped in EC 1.7.7.1. It resembled closely that of Chlorella, except for the amounts of some amino acids.

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