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Class I PurE (N5-carboxyaminoimidazole mutase) catalyzes a chemically unique mutase reaction. A working mechanistic hypothesis involves a histidine (His45 in Escherichia coli PurE) functioning as a general acid, but no evidence for multiple protonation states has been obtained. Solution NMR is a peerless tool for this task but has had limited application to enzymes, most of which are larger than its effective molecular size limit. Solid-state NMR is not subject to this limit. REDOR NMR studies of a 151 kDa complex of uniformly 15N-labeled Acetobacter aceti PurE (AaPurE) and the active site ligand [6-13C]citrate probed a single ionization equilibrium associated with the key histidine (AaPurE His59). In the AaPurE complex, the citrate central carboxylate C6 13C peak moves upfield, indicating diminution of negative charge, and broadens, indicating heterogeneity. Histidine 15N chemical shifts indicate His59 exists in approximately equimolar amounts of an Ndelta-unprotonated (pyridine-like) form and an Ndelta-protonated (pyrrole-like) form, each of which is approximately 4 A from citrate C6. The spectroscopic data are consistent with proton transfers involving His59 Ndelta that are invoked in the class I PurE mechanism.

biochemistry

Multiple Active Site Histidine Protonation States in <i>Acetobacter aceti N</i><sup>5</sup>-Carboxyaminoimidazole Ribonucleotide Mutase Detected by REDOR NMR

Multiple Active Site Histidine Protonation States in Acetobacter aceti N5-Carboxyaminoimidazole Ribonucleotide Mutase Detected by REDOR NMR

Multiple Active Site Histidine Protonation States in Acetobacter aceti N⁵-Carboxyaminoimidazole Ribonucleotide Mutase Detected by REDOR NMR