Abstract
Ferredoxin from thermophilic and mesophilic Clostridia, noting difference in heat stability due to iron and sulfide environments
Highlights
Clostridium fartarivorum and Clostridium thermosaccharolyticum, and its properties have been compared to ferredoxin from the mesophiles Closfridium pasfeurianum and Clostridium acidi urici
A number of investigations have shown that enzymes in crude extracts of thermophilic bacteria are more thermostable than corresponding enzymes in extracts of mesophilic bacteria
Pur$cation of Ferredoxin-A summary of the purification of ferredoxin from C. tartariuorum and C. thermosaccharolyticum is presented in Table 1: Repeated ammonium sulfate precipitations of the material obtained after the Sephadex G-25 step did not result in an increase in the specific activity or the A390:Aao value
Summary
Clostridium fartarivorum and Clostridium thermosaccharolyticum, and its properties have been compared to ferredoxin from the mesophiles Closfridium pasfeurianum and Clostridium acidi urici. The inactivation of ferredoxin by incubation at an elevated temperature does not involve irreversible denaturation of the protein but is caused by the release of iron and sulfide from the molecule. The difference in heat stabilities of the ferredoxins is probably due to different environments around the iron and inorganic sulfide which allow these constituents to dissociate more from the mesophile ferredoxin. The theory which is currently accepted as being most important suggests that proteins from thermophiles have an innately greater heat stability than corresponding proteins from mesophiles. A number of investigations have shown that enzymes in crude extracts of thermophilic bacteria are more thermostable than corresponding enzymes in extracts of mesophilic bacteria To show that such stability is a result of the structure of the protein, pure enzymes must be investigated
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