Atomic Resolution X-ray Structure of the Substrate Recognition Domain of Higher Plant Ribulose-bisphosphate Carboxylase/Oxygenase (Rubisco) Activase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference39 articles.
1. Rubisco activase constrains the photosynthetic potential of leaves at high temperature and CO2
2. Dissociation of Ribulose-1,5-Bisphosphate Bound to Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase and Its Enhancement by Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase Activase-Mediated Hydrolysis of ATP
3. Regulation of Rubisco activase and its interaction with Rubisco
4. Two conserved tryptophan residues are responsible for intrinsic fluorescence enhancement in Rubisco activase upon ATP binding
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1. Recent developments in the engineering of Rubisco activase for enhanced crop yield;Biochemical Society Transactions;2023-03-17
2. Rubisco and inorganic carbon assimilation;The Chlamydomonas Sourcebook;2023
3. Red Rubiscos and opportunities for engineering green plants;Journal of Experimental Botany;2022-09-02
4. Enhancing crop yield by using Rubisco activase to improve photosynthesis under elevated temperatures;Stress Biology;2021-08-18
5. Chaperone Machineries of Rubisco – The Most Abundant Enzyme;Trends in Biochemical Sciences;2020-09
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