[3][4][5] This major protein of the outer mitochondrial membrane of eukaryotes forms a voltage-dependent anion-selective channel (VDAC) that behaves as a general diffusion pore for small hydrophilic molecules.

[10] This protein contains about 280 amino acids and forms a beta barrel which spans the mitochondrial outer membrane.

First, VDAC-1 represents a new structural class of outer membrane β-barrel proteins with an odd number of strands.

Although both states allow passage of simple salts, VDAC is much more stringent with organic anions, a category into which most metabolites fall.

[15] The voltage-dependent ion channel plays a key role in regulating metabolic and energetic flux across the outer mitochondrial membrane.

It is involved in the transport of ATP, ADP, pyruvate, malate, and other metabolites, and thus communicates extensively with enzymes from metabolic pathways.

In the cytosol it activates proteolytic enzymes called caspases, which play a major role in cell death.

[20] In fact, it has been shown that antibodies that inhibit VDAC also interfere with Bax-mediated cytochrome c release in both isolated mitochondria and whole cells.