Cytochrome b6f, with one chlorophyll molecule per protein monomer, is a simple model system whose studies help achieve better understanding of non-photochemical spectral hole burning (NPHB) and single-complex spectroscopy results obtained in more complicated photosynthetic chlorophyll-protein complexes. We are reporting new data and proposing an alternative explanation for spectral dynamics that was recently observed in Cytochrome b6f using NPHB [Najafi et al., J. Phys. Chem. B 2015, 119, 6930−6940]. The relevant distribution of the tunneling parameter is a superposition of two components that are nearly degenerate in terms of the resultant NPHB yield and represent two tiers of the energy landscape responsible for NPHB. These two components likely burn competitively. However, similar values of the NPHB yield result from distinctly different combinations of barrier heights, shifts along the generalized coordinate d and/or masses of the entities involved in conformational changes m, with md 2 parameter different by a factor of ~2.5. Consequently in Cytochrome b6f fixed-temperature recovery and thermocycling experiments preferentially probe different components of the barrier-and -distributions encoded into the spectral holes. Both components most likely represent dynamics of the protein and not of the surrounding buffer/glycerol glass.