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Activator carbamino carbon to inhibitor phosphorus internuclear distances in ribulose-1,5-bisphosphate
D D Mueller1, A Schmidt, K L Pappan
1Department of Biochemistry, Kansas State University, Manhattan 66505-3702, USA.
Abstract:
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is a hexadecamer of approximately 550 kDa in most organisms. Rotational-echo double-resonance (REDOR) and transfer-echo double-resonance (TEDOR) solid-state NMR were used to obtain the average internuclear distance between the 99% 13CO2-labeled activator carbamino carbon to the phosphate phosphorus nuclei of active-site-bound 2-carboxy-D-arabinitol 1,5-bisphosphate (CABP), in freeze-quenched, lyophilized samples of confrey Rubisco. The distance 7.5 +/- 0.5 A determined by solid-state NMR is in agreement with the distance of 7.7 A inferred from the crystal-structure coordinates for spinach Rubisco-CABP-CO2-Mg2+ quaternary complex.