The kinetics of electron transfer from phyllosemiquinone (PhQ(*-)) to the iron sulfur cluster F(X) in Photosystem I (PS I) are described by lifetimes of approximately 20 and approximately 250 ns. These two rates are attributed to reactions involving the quinones bound primarily by the PsaB (PhQ(B)) and PsaA (PhQ(A)) subunits, respectively. The factors leading to a approximately 10-fold difference between the observed lifetimes are not yet clear. The peptide nitrogen of conserved residues PsaA-Leu722 and PsaB-Leu706 is involved in asymmetric hydrogen-bonding to PhQ(A) and PhQ(B), respectively. Upon mutation of these residues in PS I of the green alga, Chlamydomonas reinhardtii , we observe an acceleration of the oxidation kinetics of the PhQ(*-) interacting with the targeted residue: from approximately 255 to approximately 180 ns in PsaA-L722Y/T and from approximately 24 to approximately 10 ns in PsaB-L706Y. The acceleration of the kinetics in the mutants is consistent with a perturbation of the H-bond, destabilizing the PhQ(*-) state, and increasing the driving force of its oxidation. Surprisingly, the relative amplitudes of the phases reflecting PhQ(A)(*-) and PhQ(B)(*-) oxidation were also affected by these mutations: the apparent PhQ(A)(*-)/PhQ(B)(*-) ratio is shifted from 0.65:0.35 in wild-type reaction centers to 0.5:0.5 in PsaA-L722Y/T and to 0.8:0.2 in PsaB-L706Y. The most consistent account for all these observations involves considering reversibility of oxidation of PhQ(A)(*-) and PhQ(B)(*-) by F(X), and asymmetry in the driving forces for these electron transfer reactions, which in turn leads to F(x)-mediated interquinone electron transfer.