Rubredoxin from Clostridium perfringens: complete amino acid sequence and participation in nitrate reduction.
The complete primary structure of rubredoxin (Rd) isolated from Clostridium perfringens was sequenced to be: MKKFICDVCGYIYDPAVGDPDNGVEPGTEFKDIPDDWVCPLCGVDKSQFSETEE. The sequence was highly homologous to that of C. pasteurianum Rd but was different at 13 sites out of the total 54 amino acid residues (76% homology). It contained 1 Fe atom, 4 cysteine residues, and no labile sulfur, had a molecular weight of 6,056, and shared the general properties of classical anaerobic Rds. The pI was 4.4. The Rd was reduced with NADH in the presence of a specific NAD(P)H oxidoreductase preparation from the bacterium. The Km value of nitrate reductase for Rd as an electron-donor was 12 microM, a value comparable to that of the 13 microM for ferredoxin (Fd). These results taken together provide additional support for its role as the electron carrier in the nitrate reductase system [Seki, S., Ikeda, A., and Ishimoto, M. (1988) J. Biochem. 103, 583-584].
Seki
Y
Y
Department of Chemical Microbiology, Faculty of Pharmaceutical Sciences, Hokkaido University.
Seki
S
S
Satoh
M
M
Ikeda
A
A
Ishimoto
M
M
D000595:Amino Acid Sequence; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D003016:Clostridium perfringens / Q000032:analysis*; D005288:Ferredoxins / Q000032:analysis*; D006868:Hydrolysis; D007525:Isoelectric Focusing; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism; D009566:Nitrates / Q000378:metabolism*; D010084:Oxidation-Reduction; D011487:Protein Conformation; D012416:Rubredoxins / Q000032:analysis* / Q000378:metabolism
D005288:Ferredoxins; D009566:Nitrates; D012416:Rubredoxins; C023091:rubredoxin-NAD+ reductase; D009247:NADH, NADPH Oxidoreductases