Methylmalonyl-CoA mutase catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA, and uses a B12 derived prosthetic group, adenosylcobalamin, in order to accomplish this transfer.
The enzyme is a homodimer, located in the mitochondrial matrix.
The enzyme is 750 amino acids long, with the a metal ligand binding region to bind to the Cobalt region of adenosylcobalamin.

The enzyme works by cleaving the adenosylcobalamin C-Co(III) bond, giving the carbon and cobalt (III) atoms each an electron.
The cobalt then fluctuates between its two oxidation states: Co(II) and Co(III).
In this way the adenosylcobalamin works as a reversible free radical generator.
The cobalt therefore donates an electron back to the methylmalonyl-CoA backbone in order to transfer the coenzyme A group.
Methylmalonyl-CoA mutase catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA, and uses a B12 derived prosthetic group, adenosylcobalamin, in order to accomplish this transfer. The enzyme is a homodimer, located in the mitochondrial matrix. The enzyme is 750 amino acids long, with the a metal ligand binding region to bind to the Cobalt region of adenosylcobalamin.
The enzyme works by cleaving the adenosylcobalamin C-Co(III) bond, giving the carbon and cobalt (III) atoms each an electron. The cobalt then fluctuates between its two oxidation states: Co(II) and Co(III). In this way the adenosylcobalamin works as a reversible free radical generator. The cobalt therefore donates an electron back to the methylmalonyl-CoA backbone in order to transfer the coenzyme A group.
Methylmalonyl-CoA mutase deficiency