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The bc1 complex (bc1) is a redox-driven proton pump of the mitocondrial respiratory chain. Available structures of vertebrate bc1 have insufficient resolution to elucidate the detailed binding of ligand and solvent molecules important for understanding its function. Here we report the 2.5 Å structure of beef bc1 from a new crystal form (unit cell: 144×180×226 Å , P212121). It is now possible to assign water molecules and lipids, and to complete and correct the low resolution models. Details observed at this resolution will be presented and compared with the yeast bc1 structure solved in complex with a Fv fragment. Succinate-ubiquinone oxidoreductase is another membrane protein complex of the respiratory chain, oxidizing succinate into fumarate in the matrix and reducing quinone to quinol in the membrane. The enzyme from chicken heart mitochondria was crystallized in P212121 space group (69×83×291Å). The data were phased by molecular replacement with a polyalanine model of only the extrinsic part of E. coli fumarate reductase. Positive peaks corresponding to the three iron sulfur clusters, to the FAD, and to the heme of the membrane part were observed in a Fo-Fc map validating the solution. The model is currently being rebuilt in a 3Fo-2Fc map calculated after solvent flattening. It is possible to locate the heme iron and assign some αhelices of the membrane part. An anomalous map at Cu-K α -wavelength using the current phases shows peaks for the Fe-S clusters and heme.

Progress in the structural studies of the succinate-ubiquinone dehydrogrenase and the bc1 complex