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- W967513964 abstract "Publisher Summary This chapter discusses the preparation and properties of Clostridial Ferredoxins. Ferredoxin was first isolated from Clostridium pasteurianum . The protein functions as an electron transfer factor in the enzymatic formation of acetyl phosphate and hydrogen from pyruvate by extracts of that organism treated with diethylaminoethyl (DEAE)-cellulose and in a variety of other enzymatic reactions described. It is characterized as an iron–sulfur protein when the presence of acid-labile sulfur was recognized. Ferredoxin is found in all clostridial species that are examined. Procedures for the purification of clostridial ferredoxin are based on the acidic nature of the protein and its resultant high affinity for DEAE-cellulose, its small size relative to other proteins and resultant solubility in acetone, and the relative ease of crystallization of the protein with ammonium sulfate. Clostridial ferredoxin has a molecular weight of about 6000 and is composed of a single polypeptide chain containing 55 or fewer amino acid residues, 8 of which are cysteine. The biological activity of this protein is associated with its unusually low redox potential." @default.
- W967513964 created "2016-06-24" @default.
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- W967513964 date "1972-01-01" @default.
- W967513964 modified "2023-10-03" @default.
- W967513964 title "[38] Preparation and propertiesof clostridial ferredoxins" @default.
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- W967513964 doi "https://doi.org/10.1016/0076-6879(72)24089-7" @default.
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