Resonance Raman studies of Co-O2 and O-O stretching vibrations in oxy-cobalt hemes.

Strong evidence suggests that the stretching vibration of the bound oxygen can be perturbed by an accidentally degenerate porphyrin ring mode, resulting in two split frequencies. In the Co(II)(TpivPP) (pyridine) (18)O(2) complex, we demonstrate that the nu((18)O-(18)O) mode, after being shifted from its nu((16)O-(16)O) value at 1,156 cm(-1), undergoes a resonance interaction with the 1,080 cm(-1) porphyrin mode, giving rise to two lines at 1,067 and 1,089 cm(-1). In the O(2) complex of Co(II) mesoporphyrin IX-substituted sperm whale myoglobin, we observed a dramatic intensity increase at 1,132 cm(-1) upon (16)O(2) --> (18)O(2) substitution, which is due to the reappearance of the 1,132-cm(-1) porphyrin mode after the removal of resonance conditions. A decrease in O(2) binding affinity, caused by the proximal base tension, corresponds to an increase in the Co-O(2) stretching frequency. The nu(Co-O(2)) at 527 cm(-1) for the low affinity Co(II)(TpivPP)(1,2-Me(2)Im) O(2) complex is 11 cm(-1) higher than the 516-cm(-1) value for the high affinity complex (with N-MeIm replacing 1,2-Me(2)Im). However, in the corresponding iron complexes the reverse behavior is observed, i.e., the nu(Fe-O(2)) decreases for the (1,2-Me(2)Im) complex. There is a 24-cm(-1) difference in the Co-O(2) stretching frequencies between Co(II)(TpivPP)(N-MeIm)O(2) (at 516 cm(-1)) and oxy meso CoMb (at 540 cm(-1)), suggesting a protein induced distortion of the Co-O-O linkage. However, the values for nu(Fe-O(2)) are nearly identical between Fe(II)(TpivPP)(N-MeIm)O(2) (at 571 cm(-1)) and oxy Mb (at 573 cm(-1)), indicating that O(2) binds to myoglobin in the same manner as in the sterically unhindered "picket fence" complex. Evidence is presented that suggests the presence of two dioxygen stretching frequencies due to two different conformers in each of the N-MeIm and 1,2-Me(2)Im complex of oxy Co(II)(TpivPP).