Primary structure of a 7Fe ferredoxin from Streptomyces griseus.
The complete primary structure of a Streptomyces griseus (ATCC 13273) 7Fe ferredoxin, which can couple electron transfer between spinach ferredoxin reductase and S. griseus cytochrome P-450soy for NADPH-dependent substrate oxidation, has been determined by Edman degradation of the whole protein and peptides derived by Staphylococcus aureus V8 proteinase and trypsin digestion. The protein consists of 105 amino acids and has a calculated molecular weight, including seven irons and eight sulfurs, of 12,291. The ferredoxin sequence is highly homologous (73%) to that of the 7Fe ferredoxin from Mycobacterium smegmatis. The N-terminal half of the sequence, which is the Fe-S clusters binding domain, has more than 50% homology with other 7Fe ferredoxins. In particular, the seven cysteines known from the crystal structure of Azotobacter vinelandii ferredoxin I to be involved in binding the two Fe-S clusters are conserved.
Trower
M K
MK
E.I. du Pont de Nemours & Company Inc., Central Research and Development Department, Wilmington, DE 19880-0228.
Marshall
J E
JE
Doleman
M S
MS
Emptage
M H
MH
Sariaslani
F S
FS
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism; D005288:Ferredoxins / Q000032:analysis* / Q000378:metabolism; D007501:Iron / Q000032:analysis*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009161:Mycobacterium / Q000032:analysis; D010446:Peptide Fragments; D012689:Sequence Homology, Nucleic Acid; D012697:Serine Endopeptidases; D013305:Streptomyces griseus / Q000032:analysis*; D013455:Sulfur / Q000032:analysis; D014357:Trypsin
D000596:Amino Acids; D005288:Ferredoxins; D010446:Peptide Fragments; D013455:Sulfur; D003577:Cytochrome P-450 Enzyme System; D007501:Iron; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase; D014357:Trypsin