Abstract: | The oxygenase component of toluene dioxygenase from Pseudomonas putida F1 is an iron-sulfur protein (ISPTOL) consisting of α (TodC1) and β (TodC2) subunits. Purified TodC1 gave absorbance and electron paramagnetic resonance spectra identical to those given by purified ISPTOL. TodC1 was reduced by NADH and catalytic amounts of ReductaseTOL and FerredoxinTOL. Reduced TodC1 did not oxidize toluene, and catalysis was strictly dependent on the presence of purified TodC2. |