Purification and characterization of a [3Fe-4S][4Fe-4S] type ferredoxin from hyperthermophilic archaeon, Pyrobaculum islandicum.
A ferredoxin was purified from the hyperthermophilic archaeon, Pyrobaculum islandicum. EPR spectra and metal content analyses suggested that the ferredoxin molecule contained one [3Fe-4S] and one [4Fe-4S] cluster. The ferredoxin was rapidly reduced by 2-oxoglutarate: ferredoxin oxidoreductase purified from P. islandicum, indicating that it functions physiologically as an electron sink for the redox enzymes participating in glycolytic metabolism. Furthermore, the amino acid sequence of the P. islandicum ferredoxin was compared with those of several other bacterial ferredoxins.
Nakajima
Y
Y
Department of Bioscience, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Nagatsuta 4259, Midori-ku, Yokohama 226, Japan.
Fujiwara
T
T
Fukumori
Y
Y
D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry; D001426:Bacterial Proteins / Q000737:chemistry; D004578:Electron Spin Resonance Spectroscopy; D004586:Electrophoresis / Q000379:methods; D005288:Ferredoxins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010802:Phylogeny; D017386:Sequence Homology, Amino Acid; D019624:Thermoproteaceae / Q000737:chemistry*
D019843:Archaeal Proteins; D001426:Bacterial Proteins; D005288:Ferredoxins