Purification and characterization of NADPH-dependent Cr(VI) reductase from Escherichia coli ATCC 33456.

@article{Bae2005PurificationAC,
  title={Purification and characterization of NADPH-dependent Cr(VI) reductase from Escherichia coli ATCC 33456.},
  author={Woo-Chul Bae and Han-Ki Lee and Young-Chool Choe and D J Jahng and Sang-Hee Lee and Sang-Jin Kim and Jung-Hyun Lee and Byeong-Chul Jeong},
  journal={Journal of microbiology},
  year={2005},
  volume={43 1},
  pages={21-7}
}
A soluble Cr(VI) reductase was purified from the cytoplasm of Escherichia coli ATCC 33456. The molecular mass was estimated to be 84 and 42 kDa by gel filtration and SDS-polyacrylamide gel electrophoresis, respectively, indicating a dimeric structure. The pI was 4.66, and optimal enzyme activity was obtained at pH 6.5 and 37 degrees C. The most stable condition existed at pH 7.0. The purified enzyme used both NADPH and NADH as electron donors for Cr(VI) reduction, while NADPH was the better… CONTINUE READING

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