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We used non-photochemical persistent spectral hole-burning at 1.4 K to investigate the Qy(1,0) vibrational structure of Chl a in a water-soluble chlorophyll-binding protein (WSCP) which exhibits resolved structure in its broadband optical spectra. FranckCondon vibrational overlap factors were determined from the vibrational hole-burning data and used to simulate the Qy(1,0) spectra. The simulations were not able to accurately reproduce the details of the Qy(1,0) spectrum. This indicates a breakdown of the approximations used for the analysis and demonstrates that vibrationally induced mixing of electronic states (vibronic coupling) is active for Chl a. By considering the inhomogeneous broadening and vibrational hole-burning phenomena in the Qx and Qy(1,0) region of Chl-WSCP in addition to magnetic circular dichroism data, we favor the traditional placement of Qx at λ∼570–590 nm rather than the alternate assignment underneath the Qy(1,0) absorption near λ∼615–630 nm

The assignment of Qy(1,0) vibrational structure and Qx for chlorophyll a