Isolation and characterization of a rubredoxin and an (8Fe-8S) ferredoxin from Desulfuromonas acetoxidans.
A two cluster (4Fe-4S) ferredoxin and a rubredoxin have been isolated from the sulfur-reducing bacterium Desulfuromonas acetoxidans. Their amino acid compositions are reported and compared to those of other iron-sulfur proteins. The ferredoxin contains 8 cysteine residues, 8 atoms of iron and 8 atoms of labile sulfur per molecule; its minimum molecular weight is 6163. The protein exhibits an abosrbance ratio of A385/A283 = 0.74. Storage results in a bleaching of the chromophore; the denatured ferredoxin is reconstitutable with iron and sulfide. The instability temperature is 52 degrees C. The rubredoxin does not differ markedly from rubredoxins from other anaerobic bacteria.
D000596:Amino Acids / Q000032:analysis; D001419:Bacteria / Q000032:analysis*; D055598:Chemical Phenomena; D002621:Chemistry; D004355:Drug Stability; D005288:Ferredoxins / Q000302:isolation & purification*; D007501:Iron / Q000032:analysis; D007506:Iron-Sulfur Proteins; D008722:Methods; D012416:Rubredoxins / Q000302:isolation & purification*; D013045:Species Specificity; D013455:Sulfur / Q000032:analysis
D000596:Amino Acids; D005288:Ferredoxins; D007506:Iron-Sulfur Proteins; D012416:Rubredoxins; D013455:Sulfur; D007501:Iron