ACTIVATOR CARBAMINO CARBON TO INHIBITOR PHOSPHORUS INTERNUCLEAR DISTANCES IN RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE - A SOLID-STATE NMR-STUDY

被引：15

作者：

MUELLER, DD ^{[1
]}

SCHMIDT, A ^{[1
]}

PAPPAN, KL ^{[1
]}

MCKAY, RA ^{[1
]}

SCHAEFER, J ^{[1
]}

机构：

[1] WASHINGTON UNIV,DEPT CHEM,ST LOUIS,MO 63130

来源：

BIOCHEMISTRY | 1995年 / 34卷 / 16期

关键词：

D O I：

10.1021/bi00016a034

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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% (CO2)-C-13-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 Angstrom determined by solid-state NMR is in agreement with the distance of 7.7 Angstrom inferred from the crystal-structure coordinates for spinach Rubisco-CABP-CO2-Mg2+ quaternary complex.

引用

页码：5597 / 5603

页数：7

共 51 条

[1] CRYSTAL-STRUCTURE OF THE ACTIVE-SITE OF RIBULOSE-BISPHOSPHATE CARBOXYLASE [J].