Fig. 2: NADH-binding site in complex I.
From: Key role of quinone in the mechanism of respiratory complex I
a The main interactions of NADH with subunit Nqo1 (CXINADH structure, after short soaking). FMN is coloured in white, NADH is in salmon. Key Nqo1 residues are labelled and the main NADH–protein interactions are indicated with yellow dashes, with distances in Å. b NADH binding out of its pocket after 5 h of soaking, ~15 Å away from FMN. c A structure obtained after overnight soaking with NADH shows a flip of H384, key residue involved in the reduction of Q at the Q-site. The CXIDQ structure is overlaid and coloured in grey, illustrating potential clash of DQ with flipped H384. d Cryo-EM map section demonstrating that NADH is bound to complex I in the CXIMJ:NADH structure.
