Evidence for a redox-linked ionizable group associated with the [2Fe-2S] cluster of Thermus Rieske protein.
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.
D055598:Chemical Phenomena; D002627:Chemistry, Physical; D014450:Electron Transport Complex III; D006863:Hydrogen-Ion Concentration; D007506:Iron-Sulfur Proteins / Q000378:metabolism*; D008433:Mathematics; D008667:Metalloproteins / Q000378:metabolism*; D010084:Oxidation-Reduction; D011199:Potentiometry; D013053:Spectrophotometry; D013824:Thermus / Q000378:metabolism*
D007506:Iron-Sulfur Proteins; D008667:Metalloproteins; C037989:Rieske iron-sulfur protein; D014450:Electron Transport Complex III