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Asbt was detected using a rabbit antiserum directed against the last 14 amino acids of the carboxyl terminal of the hamster asbt protein.

The best fit of EPR species T to eq 1 is one equatorial nitrogen from an amino group and three equatorial oxygen ligands from carboxyl or phosphate groups (Table 2).

One set includes two equatorial oxygen from two water molecules, one equatorial oxygen from a carboxyl group or phosphate, and one equatorial nitrogen from an amino group.

The other set contains one equatorial oxygen from water and three equatorial oxygens from carboxyl groups or phosphate.

The best fit for the EPR species D2 to eq 1 is one equatorial oxygen from a hydroxyl group and three equatorial oxygens from carboxyl groups or phosphate.

25 MHz respectively, which can be fitted best with one amino group and three groups combined from carboxyl and phosphate groups as the equatorial ligands of the bound VO 2+on sCD39.

In accordance with metal-ATP complex coordination on other enzymes that hydrolyze ATP, like F 1 -ATPase [ 22 28 ] , the ?

- and ß-phosphate of ATP most likely bind to VO 2+while the third carboxyl group is contributed by a side-chain of aspartate or glutamate of sCD39.

Thus one amino group from lysine, one carboxyl group from aspartate or glutamate, and two oxygens from the phosphates of ADPNP serve as the equatorial ligands of sCD39 bound VO 2+in the presence of ADPNP.

The calculated g || and A || values that best matched the experimental values for species D2 suggest that one hydroxyl group and three oxygens derived from carboxyl groups and phosphates are the equatorial ligands of bound VO 2+-ADP.

Since the conformation corresponding to species D2 is found in the presence of ATP and is likely to be the conformation that releases bound VO +2-ADP, it is likely that the VO +2ligands are one phosphate and two carboxyl groups [ 25 ] .

When ADP is the substrate and generates species D1, one water molecule and a combination of three groups between carboxyl groups and phosphates serve as the equatorial ligands of bound VO 2+on sCD39.

The probable combination of carboxyl groups and phosphates for species D1 is one carboxyl group and two phosphates since VO 2+complexes ADP through two phosphates before VO 2+-ADP is bound to the enzyme.

The catalytic base attack results in cleavage of the ?

-phosphate of ATP, and one carboxyl group replaces the ?

-phosphate as a metal ligand (from species T to species D2), which is accompanied by a swap of an amino group with a hydroxyl group (S218?

The constant carboxyl group that appears in all conformations of sCD39 hydrolysis is likely contributed by D213 since it is close to S218.

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