Interaction of ribulose diphosphate carboxylase with 2-carboxyribitol diphosphate, an analogue of the proposed carboxylated intermediate in the CO2 fixation reaction
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference7 articles.
1. The Interaction of Metal Ions with Ribulose 1,5-Diphosphate Carboxylase from Spinach
2. Spinach Ribulose Diphosphate Carboxylase. I. Purification and Properties of the Enzyme*
3. Nonidentical subunits of ribulose diphosphate carboxylase
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1. The Kinetic Properties of Ribulosebisphosphate Carboxylase;Enzymatic and Model Carboxylation and Reduction Reactions for Carbon Dioxide Utilization;1990
2. D-ribulose-1,5-bisphosphate carboxylase/oxygenase: Function-dependent structural changes;Electron Microscopy Reviews;1989-01
3. Reaction-intermediate analogue binding by ribulose bisphosphate carboxylase/oxygenase causes specific changes in proteolytic sensitivity: the amino-terminal residue of the large subunit is acetylated proline.;Proceedings of the National Academy of Sciences;1988-03-01
4. Comparative affinities of the epimeric reaction-intermediate analogs 2- and 4-carboxy-D-arabinitol 1,5-bisphosphate for spinach ribulose 1,5-bisphosphate carboxylase.;Journal of Biological Chemistry;1988-03
5. 15 Preparation of Two-dimensional Arrays of Soluble Proteins as Demonstrated for Bacterial D-Ribulose-1,5-bisphosphate Carboxylase/Oxygenase;Methods in Microbiology;1988
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