Purification, amino-acid sequence and some properties of the ferredoxin isolated from Bacillus acidocaldarius.
Ferredoxin was isolated from the aerobic, thermophilic and acidophilic bacterium Bacillus acidocaldarius and its sequence of 78 amino acids completely determined by automated Edman degradation of the protein and of peptides derived from chemical cleavage between aspartic acid and proline and from enzymatic digestions. The optical spectrum of the oxidized protein has a broad maximum around 400 nm. The ferredoxin is thermostable: its absorbance begins to decrease only at incubation over 71 degrees C. The number of iron and inorganic sulphur atoms per molecule was determined to be 5.3 and 5.0, respectively. The calculated molar extinction coefficient was 23 000 M-1 X cm-1, the molecular mass of the apoferredoxin 8 872 Da. Contrary to all expectations, the sequence of B. acidocaldarius ferredoxin shows very little homology to that of B. stearothermophilus but closely resembles that of Thermus thermophilus.
Schlatter
D
D
Waldvogel
S
S
Zülli
F
F
Suter
F
F
Portmann
W
W
Zuber
H
H
D000595:Amino Acid Sequence; D001407:Bacillus / Q000032:analysis*; D002268:Carboxypeptidases; D004578:Electron Spin Resonance Spectroscopy; D010450:Endopeptidases; D005288:Ferredoxins / Q000032:analysis / Q000302:isolation & purification*; D006868:Hydrolysis; D007501:Iron / Q000032:analysis; D008666:Metalloendopeptidases; D008745:Methylation; D008970:Molecular Weight; D010455:Peptides / Q000032:analysis; D010799:Phycoerythrin / Q000032:analysis*; D010860:Pigments, Biological / Q000032:analysis*; D013455:Sulfur / Q000032:analysis; D014357:Trypsin
D005288:Ferredoxins; D010455:Peptides; D010860:Pigments, Biological; C026518:apoferredoxin; C045714:phycoerythrin 545; D010799:Phycoerythrin; D013455:Sulfur; D007501:Iron; D002268:Carboxypeptidases; D010450:Endopeptidases; C022633:serine carboxypeptidase; D014357:Trypsin; D008666:Metalloendopeptidases; C039830:peptidyl-Lys metalloendopeptidase