Results 311 to 320 of about 53,466 (334)

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
openaire   +2 more sources

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
openaire   +2 more sources

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
openaire   +2 more sources

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
openaire   +2 more sources

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.
openaire   +1 more source

Complex formation of rubisco and rubisco activase

Biophysical Journal, 2022
Kazi Waheeda, Po-Lin Chiu
openaire   +1 more source

The Hidden Face of Rubisco

Trends in Plant Science, 2018
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) fixes atmospheric CO2 into organic compounds and is composed of eight copies each of a large subunit (RbcL) and a small subunit (RbcS). Recent reports have revealed unusual RbcS, which are expressed in particular tissues and confer higher catalytic rate, lesser affinity for CO2, and a more ...
Pottier, Mathieu, Gilis, Dimitri, Boutry, Marc   +2 more
openaire   +3 more sources

Rubisco's chiropractor: a study of higher plant Rubisco activase

2015
Rubisco activase operates as the chaperone responsible for maintaining the catalytic competency of Ribulose 1,5-bisphophate carboxylase oxygenase (Rubisco) in plants. Rubisco is notoriously inefficient, rapidly self-inactivating under physiological conditions. Rubisco activase uses the power released from the hydrolysis of ATP to power a conformational
openaire   +2 more sources