Biochemical and molecular characterization of the [NiFe] hydrogenase from the hyperthermophilic archaeon, Thermococcus litoralis.

@article{Rkhely1999BiochemicalAM,
  title={Biochemical and molecular characterization of the [NiFe] hydrogenase from the hyperthermophilic archaeon, Thermococcus litoralis.},
  author={G{\'a}bor R{\'a}khely and Zhi Hao Zhou and Michael W. W. Adams and Korn{\'e}l L Kov{\'a}cs},
  journal={European journal of biochemistry},
  year={1999},
  volume={266 3},
  pages={1158-65}
}
Thermococcus litoralis is a hyperthermophilic archaeon that grows at temperatures up to 98 degrees C by fermentative metabolism and reduces elemental sulfur (S0) to H2S. A [NiFe] hydrogenase, responsible for H2S or H2 production, has been purified and characterized. The enzyme is composed of four subunits with molecular mass 46, 42, 34 and 32 kDa. Elemental analyses gave approximate values of 22 Fe, 22 S and 1 Ni per hydrogenase. EPR spectra at 70 and 5 K indicated the presence of four or five… CONTINUE READING

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