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Background  The bioenergetics of Archaea with respect to the evolution of electron transfer systems is very interesting. In contrast to terminal oxidases, a canonical  bc  1  complex has not yet been isolated from Archaea. In particular,  c -type cytochromes have been reported only for a limited number of species.    Results  Here, we isolated a  c -type cytochrome-containing enzyme complex from the membranes of the hyperthermophilic archaeon,  Aeropyrum pernix , grown aerobically. The redox spectrum of the isolated  c -type cytochrome showed a characteristic α-band peak at 553 nm corresponding to heme C. The pyridine hemochrome spectrum also revealed the presence of heme B. In non-denaturing polyacrylamide gel electrophoresis, the cytochrome migrated as a single band with an apparent molecular mass of 80 kDa, and successive SDS-PAGE separated the 80-kDa band into 3 polypeptides with apparent molecular masses of 40, 30, and 25 kDa. The results of mass spectrometry indicated that the 25-kDa band corresponded to the hypothetical cytochrome  c  subunit encoded by the ORF  APE_1719.1 . In addition, the  c -type cytochrome-containing polypeptide complex exhibited menaquinone: yeast cytochrome  c  oxidoreductase activities.    Conclusion  In conclusion, we showed that  A. pernix , a hyperthemophilic archaeon, has a "full"  bc  complex that includes a  c -type cytochrome, and to the best of our knowledge,  A. pernix  is the first archaea from which such a  bc  complex has been identified. However, an electron donor candidates for cytochrome  c  oxidase, such as a blue copper protein, have not yet been identified in the whole genome data of this archaeon. We are currently trying to identify an authentic substrate between a  bc  complex and terminal oxidase.

Purification and biochemical properties of a cytochrome bc complex from the aerobic hyperthermophilic archaeon Aeropyrum pernix