title: Mössbauer spectroscopic studies of the terminal dioxygenase protein of benzene dioxygenase from Pseudomonas putida.
abstract: 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.
mesh_terms: 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*
chemical_list: D007506:Iron-Sulfur Proteins; D008667:Metalloproteins; D006899:Mixed Function Oxygenases; C019765:benzene 1,2-dioxygenase