Redox potential of cytochrome c550 in the cyanobacterium Thermosynechococcus elongates

Cytochrome c550 (cyt c550) from photosystem II (PSII) exists in the PSII‐bound form but can be released from PSII by treatment with divalent cations or Tris, yielding the isolated form. We calculated heme redox potentials ( E m ) based on the crystal structures of cyt c550 by solving the Poisson–Boltzmann equation. In the isolated form, the calculated E m are −240 mV at pH 6.0 and −352 mV at pH 9.0. This pH‐dependence is predominantly due to deprotonation of the heme‐propionic group near Asn‐49. In the PSII‐bound form, the calculated E m was up‐shifted by 160 mV versus the isolated form due to a conformational change of protein backbone, yielding E m = −84 mV.