Properties of a thermostable 4Fe-ferredoxin from the hyperthermophilic bacterium Thermotoga maritima.
A ferredoxin has been purified from one of the most ancient and most thermophilic bacteria known, Thermotoga maritima, which grows up to 90 degrees C. The reduced protein (M(r) approx. 6300) contains a single S = 1/2 [4Fe-4S]1+ cluster with complete cysteinyl ligation, and was unaffected after incubation at 95 degrees C for 12 h. It functioned as an electron carrier for T. maritima pyruvate oxidoreductase. Remarkably, the properties and amino acid sequence of this hyperthermophilic bacterial protein are much more similar to those of ferredoxins from hyperthermophilic archaea, rather than ferredoxins from mesophilic and moderately thermophilic bacteria.
Blamey
J M
JM
Department of Biochemistry, University of Georgia, Athens 30602.
Mukund
S
S
Adams
M W
MW
D000595:Amino Acid Sequence; D005288:Ferredoxins / Q000737:chemistry / Q000302:isolation & purification*; D006089:Gram-Negative Anaerobic Bacteria / Q000737:chemistry*; D008969:Molecular Sequence Data
D005288:Ferredoxins