Excitation energy transfer in the Photosystem II core antenna complex CP43 has been investigated by vis/vis and vis/mid-IR pump-probe spectroscopy with the aim of understanding the relation between the dynamics of energy transfer and the structural arrangement of individual chlorophyll molecules within the protein. Energy transfer was found to occur on time scales of 250 fs, 2-4 ps, and 10-12 ps. The vis/mid-IR difference spectra show that the excitation is initially distributed over chlorophylls located in environments with different polarity, since two 9-keto C=O stretching bleachings, at 1691 and 1677 cm-1, are observable at early delay times. Positive signals in the initial difference spectra around 1750 and 1720 cm-1 indicate the presence of a charge transfer state between strongly interacting chlorophylls. We conclude, both from the spectral behavior in the visible when the annihilation processes are increased and from the vis/mid-IR data, that there are two pigments (one absorbing around 670 nm and one at 683 nm) which are not connected to the other pigments on a time scale faster than 10-20 ps. Since, in the IR, on a 10 ps time scale the population of the 1691 cm-1 mode almost disappears, while the 1677 cm-1 mode is still significantly populated, we can conclude that at least some of the red absorbing pigments are located in a polar environment, possibly forming H-bonds with the surrounding protein.