The plant mitochondrial cytochrome bc1 complex, like nonplant mitochondrial complexes, consists of cytochromes b and c1, the Rieske iron-sulfur protein, two Core proteins, and five low-molecular mass subunits. However, in contrast to nonplant sources, the two Core proteins are identical to subunits of the general mitochondrial processing peptidase (MPP). The MPP is a fascinating enzyme that catalyzes the specific cleavage of the diverse presequence peptides from hundreds of the nuclear-encoded mitochondrial precursor proteins that are synthesized in the cytosol and imported into the mitochondrion. Integration of the MPP into the bc1 complex renders the bc1 complex in plants bifunctional, being involved both in electron transport and in protein processing. Despite the integration of MPP into the bc1 complex, electron transfer as well as translocation of the precursor through the import channel are independent of the protein-processing activity. Recognition of the processing site by MPP occurs via the recognition of higher-order structural elements in combination with charge and cleavage-site properties. Elucidation of the three-dimensional (3-D) structure of the mammalian cytochrome bc1 complex is highly useful for understanding of the mechanism of action of MPP.