The voltage-dependent, anion-selective channel (VDAC) is generally considered the main
pathway for metabolite diffusion across the mitochondrial outer membrane. It also interacts
with several mitochondrial and cytosolic proteins, including kinases and cytochrome c.
Sequence analysis and circular dichroism suggest that the channel is a bacterial porin-like β-
barrel. However, unlike bacterial porins, VDAC does not form tight trimeric complexes and is
easily gated (reversibly closed) by membrane potential and low pH. Circular dichroism …