Ribulose-1,5-bisphosphate carboxylase/oxygenase from thermophilic red algae with a strong specificity for CO2 fixation.
about
Despite slow catalysis and confused substrate specificity, all ribulose bisphosphate carboxylases may be nearly perfectly optimizedPlastome-encoded bacterial ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO) supports photosynthesis and growth in tobaccoCrystal structure of carboxylase reaction-oriented ribulose 1, 5-bisphosphate carboxylase/oxygenase from a thermophilic red alga, Galdieria partitaStructure-based Catalytic Optimization of a Type III Rubisco from a HyperthermophileStructural mechanism of RuBisCO activation by carbamylation of the active site lysinePredicting Effects of Ocean Acidification and Warming on Algae Lacking Carbon Concentrating MechanismsHighly conserved small subunit residues influence rubisco large subunit catalysis.Phylogenetic engineering at an interface between large and small subunits imparts land-plant kinetic properties to algal RubiscoAssessment of structural and functional divergence far from the large subunit active site of ribulose-1,5-bisphosphate carboxylase/oxygenase.Avenues for genetic modification of radiation use efficiency in wheat.Electron flow to oxygen in higher plants and algae: rates and control of direct photoreduction (Mehler reaction) and rubisco oxygenase.Functional hybrid rubisco enzymes with plant small subunits and algal large subunits: engineered rbcS cDNA for expression in chlamydomonas.Catalytic by-product formation and ligand binding by ribulose bisphosphate carboxylases from different phylogenies.The possible evolution, and future, of CO2-concentrating mechanisms.Transgenic approaches to manipulate the environmental responses of the C3 carbon fixation cycle.Photorespiratory glycolate oxidase is essential for the survival of the red alga Cyanidioschyzon merolae under ambient CO2 conditionsStructural and functional similarities between a ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO)-like protein from Bacillus subtilis and photosynthetic RuBisCO.Evolution of the biochemistry of the photorespiratory C2 cycle.Maintaining photosynthetic CO2 fixation via protein remodelling: the Rubisco activases.Electron-correlated fragment-molecular-orbital calculations for biomolecular and nano systems.Temperature responses of the Rubisco maximum carboxylase activity across domains of life: phylogenetic signals, trade-offs, and importance for carbon gain.A compendium of temperature responses of Rubisco kinetic traits: variability among and within photosynthetic groups and impacts on photosynthesis modelingRubisco Catalytic Properties and Temperature Response in Crops.Isolation and kinetic characterisation of hydrophobically distinct populations of form I Rubisco.The Diverse AAA+ Machines that Repair Inhibited Rubisco Active Sites.The potential for co-evolution of CO2-concentrating mechanisms and Rubisco in diatoms.Engineering of a type III rubisco from a hyperthermophilic archaeon in order to enhance catalytic performance in mesophilic host cells.Positively selected amino acid replacements within the RuBisCO enzyme of oak trees are associated with ecological adaptationsMutation design of a thermophilic Rubisco based on three-dimensional structure enhances its activity at ambient temperature.Crystallization and Characterization of Galdieria sulphuraria RUBISCO in Two Crystal Forms: Structural Phase Transition Observed in P21 Crystal Form.Inorganic carbon acquisition in some synurophyte algae.Temperature dependence of in vitro Rubisco kinetics in species of Flaveria with different photosynthetic mechanisms.Expanding knowledge of the Rubisco kinetics variability in plant species: environmental and evolutionary trends.Revisiting RuBisCO.Presence of a structurally novel type ribulose-bisphosphate carboxylase/oxygenase in the hyperthermophilic archaeon, Pyrococcus kodakaraensis KOD1.What physiological acclimation supports increased growth at high CO2 conditions?Mechanism of CO2 acquisition in an acid-tolerant Chlamydomonas.Cytoplasmic localization of the single glutamine synthetase in a unicellular red alga, Cyanidioschyzon merolae 10D.The diversity and coevolution of Rubisco, plastids, pyrenoids, and chloroplast-based CO2-concentrating mechanisms in algaePhytosequestration: Carbon Biosequestration by Plants and the Prospects of Genetic Engineering
P2860
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P2860
Ribulose-1,5-bisphosphate carboxylase/oxygenase from thermophilic red algae with a strong specificity for CO2 fixation.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
1997年學術文章
@zh-hant
name
Ribulose-1,5-bisphosphate carb ...... specificity for CO2 fixation.
@en
Ribulose-1,5-bisphosphate carb ...... specificity for CO2 fixation.
@nl
type
label
Ribulose-1,5-bisphosphate carb ...... specificity for CO2 fixation.
@en
Ribulose-1,5-bisphosphate carb ...... specificity for CO2 fixation.
@nl
prefLabel
Ribulose-1,5-bisphosphate carb ...... specificity for CO2 fixation.
@en
Ribulose-1,5-bisphosphate carb ...... specificity for CO2 fixation.
@nl
P2093
P356
P1476
Ribulose-1,5-bisphosphate carb ...... specificity for CO2 fixation.
@en
P2093
P304
P356
10.1006/BBRC.1997.6497
P407
P577
1997-04-01T00:00:00Z