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- W2004730328 abstract "Yeast enolase binds one mole of 113Cd2+ per subunit at a site that consists of all oxyligands in a distorted octahedral environment. This conformational metal ion's environment undergoes further distortion on addition of substrate/product or analogs. At pH's below the optimum value the shifted resonance tends to break up into several, suggesting the existence of several slowly exchanging intermediate forms. At acid pH's, on addition of one additional mole/subunit of 113Cd2+, which greatly increases catalysis, conformational resonance(s) further broadens, suggesting that the second, catalytic metal ion increases the rates of interconversion between conformational species. At more alkaline pH's, near the optimum pH, the conformational peak is sharpened, which suggests that very fast interconversion is occurring. The position of the catalytic metal ion resonance also suggests all oxyligands in a distorted octahedral geometry. The catalytic resonance is often broadened to the point where it cannot be seen, suggesting rapid changes in its geometry due to interconversion of substrate and product." @default.
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- W2004730328 date "1985-05-01" @default.
- W2004730328 modified "2023-09-24" @default.
- W2004730328 title "Cadmium(II)-113 NMR studies of the mechanism of metal ion activation of yeast enolase" @default.
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- W2004730328 doi "https://doi.org/10.1016/0162-0134(85)85013-3" @default.
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