Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.2.7.1 extracted from

  • Imai, T.; Taguchi, K.; Ogawara, Y.; Ohmori, D.; Yamakura, F.; Ikezawa, H.; Urushiyama, A.
    Characterization and cloning of an extremely thermostable, Pyrococcus furiosus-type 4Fe ferredoxin from Thermococcus profundus (2001), J. Biochem., 130, 649-655.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Thermococcus profundus Q9HHD4 ferredoxin
-

Cofactor

Cofactor Comment Organism Structure
[4Fe-4S]-center enzyme contains an extremely thermostable [4Fe-4S] ferredoxin. The Fe-S cluster has three cysteines and one aspartate as the cluster ligands. The 4Fe ferredoxin is degraded to 3Fe ferredoxin during aerobic purification. The aerobically-purified ferredoxin is reversibly converted back to the [4Fe-4S] ferredoxin by the addition of ferrous ions under reducing conditions. The anaerobically-purified [4Fe-4S] ferredoxin is quite stable, little degradtion is observed over 20 h at 100°C, while the half-life of the aerobically-purified ferredoxin is 10 h at 100°C Thermococcus profundus