Conformational changes at the Qn site of the cytb6f complex may underlie catalysis.
Malone, L.A., Qian, P., Mayneord, G.E., Hitchcock, A., Farmer, D.A., Thompson, R.F., Swainsbury, D.J.K., Ranson, N.A., Hunter, … Structural superimposition of the two halves of the spinach cytb6f complex (PQ occupied Qn site and unoccupied Qn site) reveals conformational changes in the haem cn propionates and nearby residues (R207, D20) which may underlie catalysis. Subunits are coloured with the Rieske ISP (yellow), cytb6 (green), subunit IV (cyan) and cytf (magenta). The haem cn molecule is coloured deep blue and shown in stick representation, PQ molecules are coloured yellow and also shown in stick representation (*PDB ID: 6RQF).