title: Purification and characterization of Fe(III)-EDTA reductase from Bacillus sp. B-3.
abstract: Fe(III)-EDTA reductase was purified from Bacillus sp. B-3 isolated as a Fe(III)-EDTA-degrading bacterium. The purified enzyme showed a single protein band corresponding to a molecular mass of 19 kDa on SDS-PAGE, and had FMN as cofactor. It was alkali-thermostable. Its N-terminal amino acid sequence was identical with that of NADPH azoreductase from several species of Bacillus.
authors: Department of Chemical and Biological Engineering, Ube National College of Technology, Ube, Japan. emiko@ube-k.ac.jp
authors: Emiko
authors: E
authors: Shinagawa
mesh_terms: D001407:Bacillus / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D009247:NADH, NADPH Oxidoreductases / Q000302:isolation & purification* / Q000378:metabolism*; D013379:Substrate Specificity; D013696:Temperature
chemical_list: D009247:NADH, NADPH Oxidoreductases; C061239:NADH-Fe(III)EDTA oxidoreductase