Pyruvate: ferredoxin oxidoreductase from the sulfate-reducing Archaeoglobus fulgidus: molecular composition, catalytic properties, and sequence alignments

@article{Kunow1995PyruvateFO,
  title={Pyruvate: ferredoxin oxidoreductase from the sulfate-reducing Archaeoglobus fulgidus: molecular composition, catalytic properties, and sequence alignments},
  author={Jasper Kunow and Dietmar Linder and Rudolf Kurt Thauer},
  journal={Archives of Microbiology},
  year={1995},
  volume={163},
  pages={21-28}
}
Archaeoglobus fulgidus is a hyperthermophilic sulfate-reducing archaeon. In this communication we describe the purification and properties of pyruvate: ferredoxin oxidoreductase from this organism. The catabolic enzyme was purified 250-fold to apparent homogeneity with a yield of 16%. The native enzyme had an apparent molecular mass of 120 kDa and was composed of four different subunits of apparent molecular masses of 45, 33, 25, and 13 kDa, indicating and α β γ δ structure. Per mol, the enzyme… CONTINUE READING

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