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  • Title: VO2+(IV) complexes with pyruvate carboxylase: activation of oxaloacetate decarboxylation and EPR properties of enzyme-VO2+ complexes.
    Author: Werneburg BG, Ash DE.
    Journal: Biochemistry; 1997 Nov 25; 36(47):14392-402. PubMed ID: 9398157.
    Abstract:
    Chicken liver pyruvate carboxylase catalyzes a nonclassical ping-pong mechanism in which the carboxylation of biotin at subsite 1 of the active site is coupled to the biotin-dependent carboxylation of pyruvate at subsite 2. The functions of two divalent cation cofactors and at least one monovalent cation cofactor in catalysis are not well understood. The oxyvanadyl cation, VO2+ does not support phosphoryl transfer at the first subsite, and uncouples the decarboxylation of oxaloacetate at subsite 2 from the formation of ATP at subsite 1. Stimulation of this oxaloacetate decarboxylase activity in the presence of substrates and cofactors of the first subsite, including VO2+, VOADP-, Pi, and acetyl CoA, suggests that these cofactors and substrates induce the movement of carboxybiotin from the second subsite to the first subsite, where it is decarboxylated. VO2+ EPR has provided evidence for enzymic and nucleotide divalent cation binding sites within the first subsite. The EPR properties of enzyme bound VO2+ were altered by bicarbonate, suggesting that this substrate ligands directly to VO2+ at the enzymic metal site. Fluorescence quenching experiments suggest that a monovalent cation may interact with bicarbonate at the first subsite as well. The results of this study provide evidence that (i) the extrinsic metal ion cofactors interact with the substrates at the first subsite, and that (ii) divalent cations play a role in coupling catalysis at the two nonoverlapping subsites by inducing the decarboxylation of carboxybiotin at the first subsite.
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