Published: October 23, 2011Received: May 20, 2011Available on J-STAGE: October 23, 2011Accepted: July 04, 2011
Advance online publication: October 07, 2011
Revised: -
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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