Structure-Function and Nearest Neighbor Interactions of the Cytochrome b 6 f Complex
Test prediction from our (i) high resolution (2.5 Å) structure of cyanobacterial cytochrome b 6 f complex (Structure, 22, 1008-1015, 2014), and (ii) analysis of quinone/quinol traffic within the b 6 f complex (Biophys. J., 107, 1620-1628, 2014) concerning the rate-limiting step in the linear (non-cyclic) electron transport chain. It was concluded that it arises from access of plastoquinol, the electron/proton donor, to the high potential electron carriers, i. e., the Fe 2 S 2 and cytochrome f proteins. The directed motion of the quinol proceeds via a narrow channel on the lumen or electrochemically positive, p- (lumen) side of the b 6 f complex which was defined by crystal structures of the b 6 f complex with quinol analogue inhibitors (J. Mol. Biol., 370, 39-52, 2007).