Detection and classification of hyperfine-shifted 1H, 2H, and 15N resonances of the Rieske ferredoxin component of toluene 4-monooxygenase

Selective isotope labeling was employed to analyze the origin of the paramagnetically shifed 1H, 2H and 15N resonances of T4MOC, a soluble Rieske ferredoxin component of toluene 4-monooxygenase. The paramagnetic H NMR signals from T4MOC differ from those of the plant-type and vertebrate ferredoxins, and assignments of these signals to residue and atom type in T4MOC question particular 1H NMR assignments made for the Xanthobacter Rieske center. The pattern of H-bonding to the iron-sulfur cluster of T4MOC is discussed.