Lipid functions in cytochrome bc complexes: an odd evolutionary transition in a membrane protein structure.

ABSTRACT: Lipid-binding sites and properties were compared in the hetero-oligomeric cytochrome (cyt) b(6)f and the yeast bc(1) complexes that function, respectively, in photosynthetic and respiratory electron transport. Seven lipid-binding sites in the monomeric unit of the dimeric cyanobacterial b(6)f complex overlap four sites in the Chlamydomonas reinhardtii algal b(6)f complex and four in the yeast bc(1) complex. The proposed lipid functions include: (i) interfacial-interhelix mediation between (a) the two 8-subunit monomers of the dimeric complex, (b) between the core domain (cyt b, subunit IV) and the six trans membrane helices of the peripheral domain (cyt f, iron-sulphur protein (ISP), and four small subunits in the boundary 'picket fence'); (ii) stabilization of the ISP domain-swapped trans

SUBMITTER: Hasan SS 

PROVIDER: S-EPMC3497066 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature