Characterization and complete amino acid sequence of ferredoxin II from Desulfovibrio vulgaris Miyazaki.
One of 2 ferredoxins, Fd II, purified from Desulfovibrio vulgaris Miyazaki (DvM) has been characterized and its complete amino acid sequence established. Fd II is composed of 63 amino acid residues and contains 7 cysteinyl residues but has only 4 iron atoms in an iron-sulfur cluster of a standard redox potential of -405 mV. The arrangement of cysteinyl residues in the protein suggests that some cysteinyl residues are not directly involved in ligation to the iron-sulfur cluster. Homology is recognized among Fd II (DvM), Fd I (D. desulfuricans Norway), Fd I (D. africanus Benghazi), and Fd (D. gigas). Although Fd I and Fd II in DvM are poorly homologous, the C-terminal half of Fd I is fairly homologous to the N-terminal half of Fd II. Fd II is 40% as effective as Fd I as an electron carrier for pyruvate dehydrogenase coupled with hydrogenase and cytochrome c3.
Okawara
N
N
Department of Chemistry, Shizuoka University, Japan.
Ogata
M
M
Yagi
T
T
Wakabayashi
S
S
Matsubara
H
H
D000595:Amino Acid Sequence; D003574:Cytochrome c Group / Q000032:analysis; D003901:Desulfovibrio / Q000032:analysis*; D005288:Ferredoxins / Q000032:analysis*; D007501:Iron / Q000032:analysis; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010084:Oxidation-Reduction; D011768:Pyruvate Dehydrogenase Complex; D012697:Serine Endopeptidases / Q000032:analysis; D013440:Sulfides / Q000032:analysis
D003574:Cytochrome c Group; D005288:Ferredoxins; D011768:Pyruvate Dehydrogenase Complex; D013440:Sulfides; C017165:cytochrome c(3); D007501:Iron; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase