Abstract
Ferredoxin was purified to apparent homogeneity from cell extracts of the homoacetogen Peptostreptococcus productus (strain Marburg). The yield was 70 μg ferredoxin per g wet cells of P. productus. The UV-vis spectrum exhibited characteristics of a typical clostridial ferredoxin spectrum with a molar extinction coefficient ε385 of ∼30000 M-1 cm-1 and an A385/A280 ratio of 0.76. The molecular weight Mr was near 5700 as calculated from the amino acid composition. The protein contained per mol 9.9 mol iron, 8.2 mol acid-labile sulfide, and near 7 mol cysteine indicating the presence of two 4 Fe/4 S clusters. The redox potential was determined to be-410 mV. The purified ferredoxin was reduced with carbon monoxide by the carbon monoxide dehydrogenase from crude extracts and by the partially enriched enzyme of P. productus.
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Reubelt, U., Wohlfarth, G., Schmid, R. et al. Purification and characterization of ferredoxin from Peptostreptococcus productus (strain Marburg). Arch. Microbiol. 156, 422–426 (1991). https://doi.org/10.1007/BF00248721
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DOI: https://doi.org/10.1007/BF00248721