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- W1187390301 abstract "Flavodoxin (Fld) is an electron-transferring flavoprotein isolated from extracts of Clostridium pasteurianum. It replaces the electron-transferring protein, bacterial ferredoxin (Fd), in the iron-deficient cell. Flavodoxin is isolated from extracts of Peptostreptococcus elsdenii and Desulfovibrio gigas. A flavoprotein with similar properties to flavodoxin and named phytoflavin is obtained from Anacystis nidulans. This chapter discusses a phosphoroclastic and a hydrogenase assay for flavodoxin. Flavodoxin catalyzes the oxidation of pyruvate by the clastic system of C. pasteurianum with the subsequent formation of acetyl phosphate. Flavodoxin activity is related to the generation of acetyl phosphate. A ferredoxin-free extract of C. pasteurianum is used as the source of clastic enzymes, phosphotransacetylase, and hydrogenase. Hydrogenase assay measures the capacity of flavodoxin to catalyze the evolution of hydrogen gas from dithionite solutions in the presence of the enzyme hydrogenase. C. pasteurianum is grown on nitrogen gas. The purification procedure involves autolysis of cells, batch and column diethylaminoethyl (DEAE)-cellulose chromatography, or crystallization. Flavodoxin will replace ferredoxin in numerous biological reactions." @default.
- W1187390301 created "2016-06-24" @default.
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- W1187390301 date "1971-01-01" @default.
- W1187390301 modified "2023-09-25" @default.
- W1187390301 title "[169] Flavodoxin of Clostridium pasteurianum" @default.
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- W1187390301 doi "https://doi.org/10.1016/s0076-6879(71)18126-8" @default.
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