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• W2013835300 abstract "We present the results of Mössbauer and magnetization studies of [2Fe−2S]+ clusters from the wild-type and the C56S variant 2Fe-ferredoxin from Clostridium pasteurianum. At pH = 11 in Tris/Caps buffer, samples of the C56S variant contain, at 4.2 K, a 1:1 mixture of [2Fe−2S]+ clusters with valence-localized S = 1/2 (Fd1/2) and valence-delocalized S = 9/2 (Fd9/2) ground states. A spin Hamiltonian analysis of Mössbauer spectra recorded in applied fields up to 8.0 T provides the fine structure and hyperfine parameters for Fd9/2: D9/2 = −1.5 cm-1, E/D = 0.11, A = (−13, −13, −9.1) MHz, ΔEQ = 1.83 mm/s, η = 0, and δ = 0.50 mm/s. A comparative analysis of the hyperfine tensor components for Fd9/2 and Fd1/2 shows that the intrinsic A-values cannot be directly transferred from localized to delocalized systems. This result indicates that valence delocalization is accompanied by additional modifications in the electronic structure. High-temperature Mössbauer studies show an increase in the fraction of valence-delocalized clusters, from ca. 50% at 4.2 K to ca. 94% at 200 K. Magnetic susceptibility studies rule out that the delocalized fraction generated at high temperature results from a spin conversion of Fd1/2 to Fd9/2. Rather, the change in the delocalized fraction is due to a rapid increase in the intramolecular electron-transfer rate between the two iron sites of Fd1/2. Such a localization-to-delocalization transition has not been observed previously for any Fe−S cluster. The spectral features and the temperature range of the transition (≈100 K) suggest a distribution in the rate of electron transfer between the iron sites of Fd1/2 and point toward a dispersion in the values for the electronic parameters arising from the interaction of the cluster with the protein in different conformations. The rate for electron transfer between the iron sites of Fd1/2 was calculated using a quantum mechanical method which takes into account Heisenberg−Dirac−van Vleck exchange, spin-dependent resonance interaction, and vibronic trapping. By assuming a distribution in the parameters characterizing these interactions, we have been able to model the temperature dependence of the fraction of delocalized Fd1/2 molecules. Our studies suggest that electron-transfer rates in Fe−S clusters from ferredoxins may probe the conformational substates of the protein moiety." @default.
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• W2013835300 date "1999-03-31" @default.
• W2013835300 modified "2023-10-03" @default.
• W2013835300 title "Observation and Interpretation of Temperature-Dependent Valence Delocalization in the [2Fe−2S]⁺ Cluster of a Ferredoxin from <i>Clostridium pasteurianum</i>" @default.
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• W2013835300 doi "https://doi.org/10.1021/ja983980k" @default.
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