Purification and Characterization of Fe(III)-EDTA Reductase from Bacillus sp. B-3

Emiko SHINAGAWA

doi:10.1271/bbb.110397

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Purification and Characterization of Fe(III)-EDTA Reductase from Bacillus sp. B-3

Emiko SHINAGAWA

著者情報

キーワード: Fe(III)-EDTA reductase, ferric reductase, Fe(III)-EDTA, Bacillus, azoreductase

ジャーナルフリー早期公開

論文ID: 110397

DOI https://doi.org/10.1271/bbb.110397

この記事には本公開記事があります。

The final version of this article is now available: Vol. 75 (2011) , No. 10 p.2063

詳細

抄録

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.

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