The acidic domain of cytochrome c(1) in Paracoccus denitrificans, analogous to the acidic subunits in eukaryotic bc(1) complexes, is not involved in the electron transfer reaction to its native substrate cytochrome c(552)
by Castellani, M.; Havens, J.; Kleinschroth, T.; Millett, F.; Durham, B.; Malatesta, F.; Ludwig, B.
The cytochrome bc(1) complex is a key component in several respiratory pathways. One of the characteristics of the eukaryotic complex is the presence of a small acidic subunit, which is thought to guide the interaction of the complex with its electron acceptor and facilitate electron transfer. Paracoccus denitrificans represents the only example of a prokaryotic organism in which a highly acidic domain is covalently fused to the cytochrome c(1) subunit. In this work, a deletion variant lacking this acidic domain has been produced and purified by affinity chromatography. The complex is fully intact as shown by its X-ray structure, and is a dimer (Kleinschroth et al., subm.) compared to the tetrameric (dimer-of-dimer) state of the wild-type. The variant complex is studied by steady-state kinetics and flash photolysis, showing wild type turnover and a virtually identical interaction with its substrate cytochrome c(552).
- Journal
- Biochimica et Biophysica Acta-Bioenergetics
- Volume
- 1807
- Issue
- 11
- Year
- 2011
- Start Page
- 1383-1389
- URL
- https://dx.doi.org/10.1016/j.bbabio.2011.08.001
- ISBN/ISSN
- 0005-2728
- DOI
- 10.1016/j.bbabio.2011.08.001