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The structure-function relationship is at the heart of biology and majorprotein deformations are correlated to specific functions. In the case of hemeproteins, doming is associated with the respiratory function in hemoglobin andmyoglobin, while ruffling has been correlated with electron transfer processes,such as in the case of Cytochrome c (Cyt c). The latter has indeed evolved tobecome an important electron transfer protein in humans. In its ferrous form,it undergoes ligand release and doming upon photoexcitation, but its ferricform does not release the distal ligand, while the return to the ground statehas been attributed to thermal relaxation. Here, by combining femtosecond FeK-edge X-ray absorption near-edge structure (XANES) studies and femtosecond FeKalpha and Kbeta X-ray emission spectroscopy (XES), we demonstrate that thephotocycle of ferric Cyt c is entirely due to a cascade among excited spinstates of the Iron ion, causing the ferric heme to undergo doming, which weidentify for the first time. We also argue that this pattern is common to allferric haems, raising the question of the biological relevance of doming insuch proteins.

Doming and spin cascade in Ferric Haems: Femtosecond X-ray Absorption and X-ray Emission Studies