Mössbauer spectroscopic studies of the terminal dioxygenase protein of benzene dioxygenase from Pseudomonas putida.
Mössbauer spectra obtained from the terminal dioxygenase protein of the benzene dioxygenase system from Pseudomonas putida show that it contains [2Fe--2S] centres similar to those of the two-iron plant-type ferredoxins. In the oxidized form the two iron atoms within the centre are high-spin ferric but with considerable inequivalence. In the reduced form the centre contains one extra electron, and this is localized on one of the iron atoms, which becomes high-spin ferrous.
D007506:Iron-Sulfur Proteins / Q000032:analysis*; D009682:Magnetic Resonance Spectroscopy; D008667:Metalloproteins / Q000032:analysis*; D006899:Mixed Function Oxygenases; D010084:Oxidation-Reduction; D011549:Pseudomonas / Q000201:enzymology*
D007506:Iron-Sulfur Proteins; D008667:Metalloproteins; D006899:Mixed Function Oxygenases; C019765:benzene 1,2-dioxygenase