Abstract
Aquocobalamin forms a tight complex with bovines serum albumin. Evidence is presented showing that the water molecule on the sixth coordination position of aquocobalamin hydrogen bonds to histdine residues in the protein. The aquocobalamin molecule must be in a protected environment since formate only slowly reduces Co(III) aquocobalamin to cob(II)alamin(B 12r) in the bovine serum albumin-aquocobalamin complez. The specificity of aquocobalamin binding to bovine serum albumin is substantial since other aquated Co(III) complexes do not compete for the B 12-binding sites. It has already been established that Cd 2+ binds to histidine residues in bovine serum albumin. Competitive binding experiments between aquocobalamin and Cd 2+ prove the involvement of histidine and confirm the number of aquocobalamin-binding sites in bovine serum albumin.
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