High-resolution cryoEM structures of respiratory complex I in energy-transducing membranes

Respiratory complex I powers oxidative phosphorylation in mitochondria, using the reducing potential of NADH to reduce ubiquinone-10 and drive protons across an energy-transducing membrane. High-resolution cryoEM structures have provided a framework for understanding the mechanism of complex I catalysis, but controversies on how to assign functional properties to states identified in single-particle analyses are preventing progress.

Here, I will describe a versatile self-assembled membrane system we have developed to unite structure and function for complex I. By combining precise biochemical definition with high-resolution cryoEM structures in the phospholipid bilayer of coupled vesicles we showed how the structurally defined resting states regulate the enzyme's behaviour during ischaemia and reperfusion to influence physiological outcomes. Further developments of the system are now underway, working towards structural definition of the catalytic intermediates.

Hosts: Jamie Blaza, jamie.blaza@york.ac.uk and Lianne Willems, lianne.willems@york.ac.uk. 

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