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Heme charge-transfer band III is vibronically coupled to the Soret band.

A complete resonance Raman excitation profile of the heme charge-transfer band known as band III is presented. The data obtained throughout the near-infrared region show preresonance with the Q-band, but the data also clearly show the enhancement of a number of modes in the spectral region of band III. Only nontotally symmetric modes are observed to have resonance enhancement in the band III region. The observed resonance enhancements in modes of B(1g) symmetry are compared with the enhancements of those same modes in the excitation profiles of the Q-band of deoxy myoglobin, also presented here for this first time. The Q-band data agree well with the theory of vibronic coupling in metalloporphyrins (Shelnutt, J. A. J. Chem. Phys. 1981, 74, 6644-6657). The strong vibronic coupling of the Q-band of the deoxy form of hemes is discussed in terms of the enhancement of modes with both B(1g) and A(2g) symmetry. The comparison between the Q-band and band III reveals that, consistent with the theory, only modes of B(1g) symmetry are enhanced in the vicinity of band III. These results show that band III is vibronically coupled to the Soret band. The coupling of band III to modes with strong rhombic distortion of the heme macrocycle calls into question the hypothesis that the axial iron out-of-plane displacement is primarily responsible for the structure-dynamics correlations observed in myoglobin.