- Results
- This Paper
The acidic domain of cytochrome c₁ in paracoccus denitrificans, analogous to the acidic subunits in eukaryotic bc₁ complexes, is not involved in the electron transfer reaction to its native substrate cytochrome c(552).
Michela M Castellani, Jeffrey J Havens, Thomas T Kleinschroth, Francis F Millett, Bill B Durham, Francesco F Malatesta and Bernd B Ludwig
Biochim Biophys Acta 1807(11):1383-9 (2011)
PMID 21856278
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).
DOI: 10.1016/j.bbabio.2011.08.001
Version: za2963e q8za8 q8zb5 q8zc1 q8zda q8zeb q8zfa q8zga
DOI: 10.1016/j.bbabio.2011.08.001
Version: za2963e q8za8 q8zb5 q8zc1 q8zda q8zeb q8zfa q8zga