Results 31 to 40 of about 15,659 (255)
Plant Physiology, 1997 Abstract We compared the heat-denaturation profiles of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) and Rubisco activase and further examined the ability of Rubisco activase to restore the activity of heat-denatured Rubisco originally reported (E. Sanchez de Jimenez, L. Medrano, and E. Martinez-Barajas [1995] Biochemistry 34:
Nancy A. Eckardt, Archie R. Portis
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Regulation of Rubisco activase and its interaction with Rubisco [PDF]
Journal of Experimental Botany, 2007 The large, alpha-isoform of Rubisco activase confers redox regulation of the ATP/ADP response of the ATP hydrolysis and Rubisco activation activities of the multimeric activase holoenzyme complex. The alpha-isoform has a C-terminal extension that contains the redox-sensitive cysteine residues and is characterized by a high content of acidic residues ...
Archie R. Portis +3 more
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Investigating the Stoichiometry of RuBisCO Activase by Fluorescence Fluctuation Methods [PDF]
Biophysical Journal, 2012 Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is an enzyme that catalyzes the carboxylation of the substrate Ribulose-1,5-bisphosphate. The notorious inefficiency of RuBisCO to catalyze carboxylation is due to inhibition by various metabolites. RuBisCO activase, an ancillary enzyme is needed to foster the activity of RuBisCO.
Manas Chakraborty +4 more
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Boundaries of photosynthesis: adaptations of carbon fixation in extreme environments. [PDF]
FEBS Open BioPhotosynthesis faces challenges from environmental extremes of temperature, pH, and salinity, limiting gas diffusion, modifying membrane fluidity, and destabilizing photochemical and biochemical reactions. Photosynthetic organisms have evolved unique adaptations overcoming these stresses and maintaining their photosynthetic activity.
Aguiló-Nicolau P +3 more
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Antisense Inhibition of Rubisco Activase Increases Rubisco Content and Alters the Proportion of Rubisco Activase in Stroma and Thylakoids in Chloroplasts of Rice Leaves [PDF]
Annals of Botany, 2006 Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) activase (RCA) is a nuclear-encoded chloroplast protein that modifies the conformation of Rubisco, releases inhibitors from active sites, and increases enzymatic activity. It appears to have other functions, e.g.
Songheng Jin +3 more
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Rubisco, Rubisco activase, and global climate change [PDF]
Journal of Experimental Botany, 2008 Global warming and the rise in atmospheric CO(2) will increase the operating temperature of leaves in coming decades, often well above the thermal optimum for photosynthesis. Presently, there is controversy over the limiting processes controlling photosynthesis at elevated temperature.
David S. Kubien +2 more
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Plant Physiology, 2021 Rubisco limits C3 photosynthesis under some conditions and is therefore a potential target for improving photosynthetic efficiency. The overproduction of Rubisco is often accompanied by a decline in Rubisco activation, and the protein ratio of Rubisco ...
Mao Suganami +4 more
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Effects of OsRCA Overexpression on Rubisco Activation State and Photosynthesis in Maize
Plants, 2023 Ribulose–1,5–bisphosphate carboxylase/oxygenase (Rubisco) is the rate–limiting enzyme for photosynthesis. Rubisco activase (RCA) can regulate the Rubisco activation state, influencing Rubisco activity and photosynthetic rate. We obtained transgenic maize
Yujiao Feng +4 more
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Regulation of ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) activase: product inhibition, cooperativity, and magnesium activation. [PDF]
J Biol Chem, 2015 Hazra S +4 more
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The Plant Journal, 2022 Our previous study revealed that the transcription factor Ghd2 increases rice yield potential under normal conditions and accelerates leaf senescence under drought stress.
Xiaowei Fan +6 more
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