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• W1520463777 abstract "The [2Fe-2S] clusters of Thermus Rieske protein, which were previously found to have nitrogen atoms coordinated directly to the iron (Cline, J.F., Hoffman, B.M., LaHaie, E., Ballou, D.P., and Fee, J.A. (1985) J. Biol. Chem. 260, 3251-3254), are now shown to have a tightly linked ionization that affects the spectral and redox properties of the cluster. The data are consistent with the reactions LH+, Fe3+ in equilibrium with L-Fe3+ +H+ and L-Fe3+ + H+ + e in equilibrium with LH+, Fe2+, where L is coordinated to Fe3+ but LH+ may not be, depending on its structure. The pKa of the protonic equilibrium is approximately 8 and the midpoint potential, Em7, is approximately 140 mV. Possible structures of L are suggested." @default.
• W1520463777 created "2016-06-24" @default.
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• W1520463777 date "1986-02-01" @default.
• W1520463777 modified "2023-09-30" @default.
• W1520463777 title "Evidence for a redox-linked ionizable group associated with the [2Fe-2S] cluster of Thermus Rieske protein." @default.
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• W1520463777 doi "https://doi.org/10.1016/s0021-9258(17)35851-9" @default.
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