The pH- and the temperature dependence of the rate constant for electron transfer from tyrosine to ruthenium in Ru(II)(bpy)(2)(4-Me-4'CONH-L-tyrosine etyl ester-2,2'-bpy) 2PF(6) was investigated using flash photolysis. At a pH below the tyrosine pK(a) approximate to 10 the rate constant increased monotonically with pH. This increase was consistent with a concerted electron transfer/deprotonation mechanism. Also indicative of a concerted reaction was the unusually high reorganization energy, 2 eV, extracted from temperature-dependent measurements. Deprotonation of the tyrosine group, at pH > pK(a), resulted in a 100-fold increase in rate constant due to a decreased reorganization energy, lambda = 0.9 eV. Also, the rate constant became independent of pH, In Mn-depleted photosystem II a similar pH dependence has been found for electron transfer from tyrosine(Z) (Tyr(Z)) to the oxidized primary donor P680(+). On the basis of the kinetic similarities we propose that the mechanisms in the two systems are the same, that is, the electron transfer occurs as a concerted proton-coupled electron-transfer reaction, and at pH < 7 the Tyr(Z) proton is released directly to the bulk water.