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Inactivation of Nitrate Reductase of the Yeast, Rhodotorula glutinis
Author(s) -
ITO NOBUAKI,
SUZUKI YONEZO
Publication year - 1978
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1978.tb01606.x
Subject(s) - nitrate reductase , rhodotorula , hydroxylamine , nitrate , chemistry , biochemistry , yeast , ammonium , reductase , enzyme , organic chemistry
Nitrate reductase (NR) from the yeast, Rhodotorula glutinis var. salinaria was composed of two enzymatic components, diaphorase and terminal nitrate reducing moieties. The enzyme used NADPH as electron donor and FAD as cofactor. The synthesis of nitrate reductase was promoted specifically by nitrate and repressed by ammonium and amino acids. Nitrate reductase from this yeast had an inactive as well as an active form. Inactive enzyme was reactivated by oxidation with ferricyanide in vitro . Hydroxylamine promoted the formation of inactive enzyme in vivo . Ammonium could neither promote the inactivation nor reduce the total level of nitrate reductase activity. Nitrate could protect nitrate reductase from inactivation caused by nitrogen starvation or hydroxylamine.