Shinagawa Emiko
Department of Chemical and Biological Engineering, Ube National College of Technology, Ube, Japan.
Biosci Biotechnol Biochem. 2011;75(10):2063-5. doi: 10.1271/bbb.110397. Epub 2011 Oct 7.
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.
从作为铁（III）-乙二胺四乙酸（EDTA）降解菌分离出的芽孢杆菌属B-3中纯化出铁（III）-EDTA还原酶。纯化后的酶在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（SDS-PAGE）上显示出一条对应于分子量为19 kDa的单一蛋白条带，并且以黄素单核苷酸（FMN）作为辅因子。它具有碱热稳定性。其N端氨基酸序列与几种芽孢杆菌属的NADPH偶氮还原酶的序列相同。
