The propensity of hexagonal II phase formation plays an important role in the activity of mitochondrial ubiquinol-cytochrome c reductase or H(+)-ATPase. The respiratory control ratio of reconstituted ubiquinol-cytochrome c reductase or the ATP-induced membrane potential of reconstituted H(+)-ATPase became higher as the non-bilayer phospholipid phosphatidylethanolamine content of proteoliposomes increased. The highest respiratory control ratio or ATP-induced membrane potential was obtained in the case of 60-80% phosphatidylethanolamine-containing proteoliposomes. Dioleoylphosphatidylethanolamine could significantly enhance the respiratory control ratio of ubiquinol-cytochrome c reductase and ATP-induced membrane potential of H(+)-ATPase, while no obvious change could be observed when dielaidoylphosphatidylethanolamine was used. The bilayer to hexagonal II phase transition temperature of ubiquinol-cytochrome c reductase-containing proteoliposomes reconstituted with phosphatidylcholine+phosphatidylethanolamine increases with decreasing content of phosphatidylethanolamine. Several additives such as the bilayer stabilizers, cholesterol 3-sulfate and carbobenzoxy-D-Phe-L-PheGly, or hexagonal II phase-forming promoters, such as diolein or eicosane, can decrease or increase the activity of these two enzyme complexes.