Transmembrane signaling and assembly of the cytochrome b6f-lipidic charge transfer complex.

ABSTRACT: Structure-function properties of the cytochrome b6f complex are sufficiently unique compared to those of the cytochrome bc1 complex that b6f should not be considered a trivially modified bc1 complex. A unique property of the dimeric b6f complex is its involvement in transmembrane signaling associated with the p-side oxidation of plastoquinol. Structure analysis of lipid binding sites in the cyanobacterial b6f complex prepared by hydrophobic chromatography shows that the space occupied by the H transmembrane helix in the cytochrome b subunit of the bc1 complex is mostly filled by a lipid in the b6f crystal structure. It is suggested that this space can be filled by the domain of a transmembrane signaling protein. The identification of lipid sites and likely function defines the intra-membra

SUBMITTER: Saif Hasan S 

PROVIDER: S-EPMC4029431 | biostudies-literature | 2013 Nov-Dec

REPOSITORIES: biostudies-literature