Properties of the iron--sulphur proteins of the benzene dioxygenase system from Pseudomonas putida.
A purification procedure was developed to stabilize the iron-sulphur proteins of the benzene dioxygenase system from Pseudomonas putida. The intermediate electron-carrying protein has a mol. wt. of 12300 and possesses one (2Fe--2S) cluster, whereas the terminal dioxygenase has a mol.wt. of 215300 and possesses two (2Fe--2S) clusters. The order and stoicheiometry of electron transfer and of the whole system are described.
D001555:Benzene Derivatives; D055598:Chemical Phenomena; D002621:Chemistry; D004579:Electron Transport; D004591:Electrophoresis, Polyacrylamide Gel; D007506:Iron-Sulfur Proteins / Q000302:isolation & purification; D008667:Metalloproteins / Q000302:isolation & purification; D006899:Mixed Function Oxygenases / Q000302:isolation & purification; D008970:Molecular Weight; D011549:Pseudomonas / Q000201:enzymology*; D013053:Spectrophotometry
D001555:Benzene Derivatives; D007506:Iron-Sulfur Proteins; D008667:Metalloproteins; D006899:Mixed Function Oxygenases