EPR spectra attributed to the redox active tyrosine residues on the oxidizing side of photosystem II (TyrZ and TyrD) have almost identical line shapes, although the tyrosyl radicals differ in stability and redox characteristics. Strongly modified spectra of oxidized TyrD in site-directed mutants in a histidine residue, H189 on the D2 reaction center protein in the cyanobacterium Synechocystis 6803, support a structural model where H189 interacts closely, probably via a hydrogen bond, to TyrD (Tommos, C., Davidsson, L., Svensson, B., Madsen, C., Vermass, W., and Styring, S. (1993) Biochemistry 32, 5436-5441). To determine whether TyrZ and the corresponding histidine on the D1 protein (D1-H190) interacts similarly, we have generated His-Phe (H190F) and His-Tyr (H190Y) mutations in the C2 symmetry related H190 residue on the D1 reaction center protein by site-directed mutagenesis in Chlamydomonas reinhardtii. The H190F and H190Y mutants assemble photosystem II reaction centers capable of primary photochemistry but unable to oxidize water. We have obtained kinetic spectra of a flash-induced transient EPR signal that we assign to oxidized TyrZ in the D1-H190 mutants. The spectra are identical in line width (18-20 G) and hyperfine structure to the wild-type spectrum from oxidized TyrZ and exhibit decay kinetics (t 1/2 approximately 500 ms) typical for the TyrZ radical in managenese-depleted photosystem II membranes. However, both TyrZ and TyrD were oxidized with reduced (10-15%) quantum yield in these mutants, indicating that the kinetics of electron donation to P+680 were significantly modified as a result of the mutation. Thus, the altered kinetics of TyrZ in the mutants suggest that there is an interaction between TyrZ and His-190 on the D1 protein. However, unlike the situation on the D2 side, the presence of a hydrogen bond between TyrZ and H190 on the D1 protein is improbable.