Results 191 to 200 of about 20,183 (216)

Rubisco: Structure and Mechanism

Annual Review of Biophysics and Biomolecular Structure, 1992
CONTENTS PERSPECTIVES AND OVERVIEW 1 1 9 PHYSIOLOGICAL AND GENETIC ASPECTS 120 Photosynthesis and Photorespiration 120 Synthesis and Assembly . . . . . ..... ... . . ... . . . . . . . . . . .. .. 121 CHEMICAL MECHANISM 122 Activation-the Ternary Complex of Enzyme, CO" and Mg( II) 122 Overall Carboxylation Reaction . . . ... . . . . . .
G, Schneider, Y, Lindqvist, C I, Brändén   +2 more
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The regulation of Rubisco by Rubisco activase

Journal of Experimental Botany, 1995
Abstract The activity of Rubisco depends on the conversion of the inactive form (E) to the active form (ECM); the binding of the inhibitors CA1P and RuBP to ECM and E, respectively; and the catalytic formation of inhibitory sugar bisphosphates from the enediol intermediate that precedes carboxylation/oxygenation.
openaire   +1 more source

The activity of Rubisco’s molecular chaperone, Rubisco activase, in leaf extracts

Photosynthesis Research, 2011
Rubisco frequently undergoes unproductive interactions with its sugar-phosphate substrate that stabilize active sites in an inactive conformation. Restoring catalytic competence to these sites requires the "molecular chiropractic" activity of Rubisco activase (activase).
Carmo-Silva, A. Elizabete, Salvucci, Michael E.   +1 more
openaire   +2 more sources

Rubisco Activase Activity Assays

2010
Ribulose-1,5-bisphosphate (RuBP) carboxylase/oxygenase (Rubisco) activase functions as a mechano-chemical motor protein using the energy from ATP hydrolysis to contort the structure of its target protein, Rubisco. This action modulates the activation state of Rubisco by removing tightly-bound inhibitory sugar-phosphates from Rubisco's catalytic sites ...
Barta, Csengele, Carmo-Silva, A. Elizabete, Salvucci, Michael E.   +2 more
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Putting the RuBisCO pieces together

Science, 2017
Scientists find a way to build the major plant enzyme RuBisCO in ...
Todd O, Yeates, Nicole M, Wheatley
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Sectioned RuBisCO crystals in TEM

Micron and Microscopica Acta, 1990
RuBisCO (D-ribulose-l,5-biphosphate carboxylase/oxygenase) is the most aboundant enzyme in the plant cell and it catalyses the key carboxylation reaction of photosynthetic carbon fixation, but also the competing oxygenase reaction of photorespiation.
Gunnel Karlsson, Jan-Olov Bovin, Michael Bosma   +2 more
openaire   +1 more source

Structure and function of Rubisco

Plant Physiology and Biochemistry, 2008
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is the major enzyme assimilating CO(2) into the biosphere. At the same time Rubisco is an extremely inefficient catalyst and its carboxylase activity is compromised by an opposing oxygenase activity involving atmospheric O(2).
Inger, Andersson, Anders, Backlund
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The Rubisco subunit binding protein

Photosynthesis Research, 1988
Chloroplasts contain an abundant soluble protein that binds non-covalently newly synthesized large and small subunits of the enzyme ribulose bisphosphate carboxylase-oxygenase. This binding protein has been purified from Pisum sativum and Hordeum vulgare in the form of a dodecamer consisting of equal amounts of two types of subunit.
R J, Ellis, S M, Van Der Vies
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Designs on Rubisco

Nature, 2006
Rubisco is said to be both the most important enzyme on Earth and surprisingly inefficient. Yet an understanding of the reaction by which it fixes CO2 suggests that evolution has made the best of a bad job.
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Complex formation of rubisco and rubisco activase

Biophysical Journal, 2022
Kazi Waheeda, Po-Lin Chiu
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