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Photosynthetic reaction centers from  Blastochloris viridis  possess Tyr-L162 located mid-way between the special pair chlorophyll (P) and the heme (heme3). While mutation of the tyrosine does not affect the kinetics of electron transfer from heme3 to P, recent time-resolved Laue diffraction studies reported displacement of Tyr-L162 in response to the formation of the photo-oxidized P +• , implying a possible tyrosine deprotonation event. p K   a  values for Tyr-L162 were calculated using the corresponding crystal structures. Movement of deprotonated Tyr-L162 toward Thr-M185 was observed in P +•  formation. It was associated with rearrangement of the H-bond network that proceeds to P via Thr-M185 and His-L168.

Tyrosine Deprotonation and Associated Hydrogen Bond Rearrangements in a Photosynthetic Reaction Center