The ultrafast response of cytochrome bc1 is investigated for the first time, via transient absorption spectroscopy. The distinct redox potentials of both c(1)- and b-hemes allow for a clear differentiation of their respective signals. We find that while the c(1)-heme photo-product exhibits the characteristics of a 5-coordinated species, the b-hemes presumably undergo photo-oxidation at a remarkably high quantum yield. The c(1)-heme iron-ligand recombination time is 5.4 ps, in agreement with previous reports on homologous cytochromes. The suggested photo-oxidized state of the b-hemes has a lifetime of 6.8 ps. From this short life-time we infer that the electron acceptor must be within van der Walls contact with the heme, which points to the fact that the axial histidine residue is the electron acceptor. The different heme-responses illustrate the flexibility of the c(1)-heme ligation in contrast to the more rigid b-heme binding, as well as the higher electronic reactivity of the b-hemes within the bc(1) complex. This study also demonstrates the remarkable connection between the heme local environment and its dynamics and, therefore, biological function.