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Papers In Press, published online ahead of print December 17, 2001
J. Biol. Chem, 10.1074/jbc.C100664200
Submitted on November 19, 2001
Revised on December 13, 2001
Accepted on December 15, 2001

The interaction of the Rieske iron sulfur protein with occupants of the Qo-site of the bc1 complex, probed by 1D and 2D electron spin echo envelope modulation

Rimma I. Samoilova, Derrick Kolling, Taketoshi Uzawa, Toshio Iwasaki, Antony R. Crofts, and Sergei A. Dikanov

Illinois EPR Center, University of Illinois at Urbana-Champaign, Urbana, IL 61801

Corresponding Author: dikanov{at}uiuc.edu

The bifurcated reaction at the Qo-site of the bc1 complex provides the mechanistic basis of the proton-pumping activity through which the complex conserves redox energy in the proton gradient. Structural information about the binding of quinone at the site is lacking because the site is vacant in crystals of the native complexes. We now report the first structural characterization of the interaction of the native quinone occupant with the Rieske iron sulfur protein in the bc(sub1) complex of Rhodobacter sphaeroides, using high resolution EPR. We have compared the binding configuration in the presence of quinone with the known structures for the complex with stigmatellin and myxothiazol. We have shown by using EPR and orientation selective ESEEM measurements of the iron sulfur protein that when quinone is present in the site, the isotropic hyperfine constant of one of the N{delta} atoms of a liganding histidine of the [2Fe-2S] cluster is similar to that observed when stigmatellin is present, and different from the configuration in the presence of myxothiazol. The spectra also show complementary differences in nitrogen quadrupole splittings in some orientations. We suggest that the EPR characteristics, the ESEEM spectra, and the hyperfine couplings reflect a similar interaction between the iron sulfur protein and the quinone or stigmatellin, and that the N{delta} involved is that of a histidine (equivalent to His-161 in the chicken mitochondrial complex) that forms both a ligand to the cluster and a hydrogen bond with a carbonyl O-atom of the Qo-site occupant.


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