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Activator Carbamino Carbon to Inhibitor Phosphorus Internuclear Distances in Ribulose-1,5-bisphosphate Carboxylase/Oxygenase. A Solid-State NMR Study

1995; American Chemical Society; Volume: 34; Issue: 16 Linguagem: Inglês

10.1021/bi00016a034

1943-295X

Delbert D. Mueller, Asher Schmidt, Kirk L. Pappan, Robert A. McKay, Jacob Schaefer,

Enzyme Structure and Function

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.