Giuseppe Amodeo

Highlights • β-NADH binding to hVDAC-1 does not change conformation of N-terminal helices • β-NADH binding leads to low VDAC conductance by sterically blocking anion flux • Elevated dynamics of the N-terminal helices are present in the ground state • Movements of helix α2 are important for VDAC gating Summary The voltage-dependent anion channel (VDAC) forms the primary diffusion pore of the outer mitochondrial membrane. In its apo form, VDAC adopts an open conformation with high conductance.