Pseudomonas putidaおよびNitrosomonas europaeaにおけるヒドロキシルアミン存在下でのシトクロムcの還元とヒドロキシルアミンの酸化

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The hydroxylamine-cytochrome c reducing acitivity and hydroxylamine-oxidizing acitivity of Pseudomonas putida and Nitrosomonas europaea were investigated by comparative assessments of the subcellular fractions in which these activities are recovered and of the enzymatic characteristics thereof. Hydroxylamine-cytochrome c reducing activity of P. putida was demonstrated in a fraction precipitating between 20 and 35% saturation with ammonium sulfate of a cell-free extract. Hydroxylamine-oxidizing acitivity of the organism was recovered in an insoluble fraction of cell-free extract only from cultures induced with hydroxylamine. Both activities of N. europaea were recovered in a fraction precipitating between 60 and 80% ammonium sulfate saturation of the cell-free extract. Slight differences were noted between P. putida and N. europaea in the enzymatic characteristics of hydroxylamine-cytochrome c reducing activity, particularly the optimal reaction temperature and pH as well as stability to heat and pH. As for stability to heat, the activity of N. europaea was stable at temperatures up to 60℃ but virtually complete inactivation occurred at 40℃ in the case of P. putida. In the presence of potassium ferricyanide, nevertheless, P. putida and N. europaea had a common tendency to prolongation of the delay in the onset of cytochrome c reduction with increasing reaction concentration. Our data suggested that the activities of P. putida may be separate enzyme proteins but the same enzyme protein catalyzes the reactions for the activities of N. europaea.
公益社団法人日本生物工学会の論文
1990-05-25

Pseudomonas putidaおよびNitrosomonas europaeaにおけるヒドロキシルアミン存在下でのシトクロムcの還元とヒドロキシルアミンの酸化

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