Purification and characterization of an iron-nickel hydrogenase from Thermococcus celer

@article{Blamey2001PurificationAC,
  title={Purification and characterization of an iron-nickel hydrogenase from Thermococcus celer},
  author={Jenny M Blamey and Mario Chiong and Eugene T. Smith},
  journal={JBIC Journal of Biological Inorganic Chemistry},
  year={2001},
  volume={6},
  pages={517-522}
}
Thermococcus celer cells contain a single hydrogenase located in the cytoplasm, which has been purified to apparent homogeneity using three chromatographic steps: Q-Sepharose, DEAE-Fast Flow, and Sephacryl S-200. In vitro assays demonstrated that this enzyme was able to catalyze the oxidation as well as the evolution of H2. T. celer hydrogenase had an apparent MW of 155,000±30,000 by gel filtration. When analyzed by SDS polyacrylamide gel electrophoresis a single band of 41,000±2000 was… CONTINUE READING