نتایج جستجو برای: rubisco

تعداد نتایج: 1869  

2017
Robert E. Sharwood Kristine Y. Crous Spencer M. Whitney David S. Ellsworth Oula Ghannoum

Leaf-level photosynthetic processes and their environmental dependencies are critical for estimating CO2 uptake from the atmosphere. These estimates use biochemical-based models of photosynthesis that require accurate Rubisco kinetics. We investigated the effects of canopy position, elevated atmospheric CO2 [eC; ambient CO2 (aC)+240 ppm] and elevated air temperature (eT; ambient temperature (aT...

Journal: :Proceedings of the National Academy of Sciences 2009

Journal: :The Biochemical journal 2008
María-Jesús García-Murria Saeid Karkehabadi Julia Marín-Navarro Sriram Satagopan Inger Andersson Robert J Spreitzer Joaquín Moreno

Proximal Cys(172) and Cys(192) in the large subunit of the photosynthetic enzyme Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase; EC 4.1.1.39) are evolutionarily conserved among cyanobacteria, algae and higher plants. Mutation of Cys(172) has been shown to affect the redox properties of Rubisco in vitro and to delay the degradation of the enzyme in vivo under stress conditions. Here, w...

Journal: :Plant, cell & environment 2007
Rowan F Sage David S Kubien

We review the current understanding of the temperature responses of C(3) and C(4) photosynthesis across thermal ranges that do not harm the photosynthetic apparatus. In C(3) species, photosynthesis is classically considered to be limited by the capacities of ribulose 1.5-bisphosphate carboxylase/oxygenase (Rubisco), ribulose bisphosphate (RuBP) regeneration or P(i) regeneration. Using both theo...

Journal: :Plant physiology 1989
M S Dann E J Pell

The effect of ozone (O(3)) on ribulose bisphosphate carboxylase/oxygenase (Rubisco) activity and quantity and net photosynthesis in greenhouse-grown Solanum tuberosum L. cv ;Norland' foliage was studied in relation to oxidant-induced premature senescence. Plants, 26 days old, were exposed to 0.06 to 0.08 microliters per liter O(3) from 1000 to 1600 hours for 4 days in a controlled environment c...

Journal: :The Journal of biological chemistry 2007
Benedict M Long Murray R Badger Spencer M Whitney G Dean Price

In cyanobacteria, the key enzyme for photosynthetic CO(2) fixation, ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco), is bound within proteinaceous polyhedral microcompartments called carboxysomes. Cyanobacteria with Form IB Rubisco produce beta-carboxysomes whose putative shell proteins are encoded by the ccm-type genes. To date, very little is known of the protein-protein interaction...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2010
Yonatan Savir Elad Noor Ron Milo Tsvi Tlusty

Rubisco (D-ribulose 1,5-bisphosphate carboxylase/oxygenase), probably the most abundant protein in the biosphere, performs an essential part in the process of carbon fixation through photosynthesis, thus facilitating life on earth. Despite the significant effect that Rubisco has on the fitness of plants and other photosynthetic organisms, this enzyme is known to have a low catalytic rate and a ...

Journal: :Bioscience, Biotechnology, and Biochemistry 2017

2017
Juan A. Perdomo Sebastià Capó-Bauçà Elizabete Carmo-Silva Jeroni Galmés

To understand the effect of heat and drought on three major cereal crops, the physiological and biochemical (i.e., metabolic) factors affecting photosynthesis were examined in rice, wheat, and maize plants grown under long-term water deficit (WD), high temperature (HT) and the combination of both stresses (HT-WD). Diffusional limitations to photosynthesis prevailed under WD for the C3 species, ...

Journal: :Plant & cell physiology 2006
Daniel Emlyn-Jones Fiona J Woodger G Dean Price Spencer M Whitney

In most cyanobacteria, the gene rbcX is co-transcribed with the rbcL and rbcS genes that code for the large and small subunits of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco). Previous co-expression studies in Escherichia coli of cyanobacterial Rubisco and RbcX have identified a chaperonin-like function for RbcX. The organization of the rbcLXS operon has, to a certain extent, precl...

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