Characterization of long-range electron transfer in mixed-metal [zinc,iron] hybrid hemoglobins.
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Measurements characterizing electron transfer from a photoexcited zinc protoporphyrin triplet (3ZnP) to a ferriheme electron acceptor within the [alpha 1,beta 2] electron-transfer complex of [FeIII,Zn] hybrid hemoglobins are reported. Analytical results demonstrate that the hybrids studied are pure, homogeneous proteins with 1:1 ZnP:FeP content. Within the T quaternary structure adopted by these hybrids, the optical spectrum of a FeIIIP is perturbed by the protein environment. Room temperature kinetic studies of the rate of 3ZnP decay as a function of the heme oxidation and ligation state demonstrate that quenching of 3ZnP by FeIII(H2O)P occurs by long-range intramolecular electron transfer with rate constant kt = 100 (+/- 10) s-1 and is not complicated by spin-quenching or energy-transfer processes; results are the same for alpha(Zn) and beta(Zn) hybrids. Replacement of H2O as a ligand to the ferriheme changes the 3ZnP----FeIIIP electron-transfer rate constant, kt, which demonstrates that electron transfer, not conformational conversion, is rate limiting. However, the trend is not readily explained by simple considerations of spin-state and bonding geometry: kt decreases in the order imidazole greater than H2O greater than F- approximately CN- approximately N3-. The reverse electron-transfer process FeIIP----ZnP+ has not been observed directly but has been shown to be much more rapid, with rate constant kb greater than 10(3) s-1, consistent with the possible importance of "hole" superexchange in electron tunneling within protein complexes.
author list (cited authors)
McGourty, J. L., Peterson-Kennedy, S. E., Ruo, W. Y., & Hoffman, B. M.
complete list of authors
McGourty, JL||Peterson-Kennedy, SE||Ruo, WY||Hoffman, BM