Results 21 to 30 of about 27,922 (261)

Activation of ribulose 1,5‐bisphosphate carboxylase by Ca²⁺ [PDF]

FEBS Letters, 1983
Purified RuBP carboxylase requires activation by reaction with CO2 and a divalent metal ion. Mg2+ is the most effective metal ion, and is probably involved in activation in vivo. Ca2+ is reported not to be an activator. Several oxyanions, including phosphate esters, are effectors of activation of RuBP carboxylase by Co2 and Mg2+.
Parry, Martin A J, Schmidt, C. N Godfrey, Keys, Alfred J., Gutteridge, Steven   +3 more
openaire   +2 more sources

Exploring the oxygenase function of Form II Rubisco for production of glycolate from CO2

AMB Express, 2021
The oxygenase activity of Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) converts ribulose-1,5-bisphosphate (RuBP) into 2-phosphoglycolate, which in turn channels into photorespiration, resulting in carbon and energy loss in higher plants.
Fan Yang, Junli Zhang, Zhen Cai, Jie Zhou, Yin Li   +4 more
doaj   +1 more source

Interactions Between Carbon Metabolism and Photosynthetic Electron Transport in a Chlamydomonas reinhardtii Mutant Without CO2 Fixation by RuBisCO

Frontiers in Plant Science, 2022
A Chlamydomonas reinhardtii RuBisCO-less mutant, ΔrbcL, was used to study carbohydrate metabolism without fixation of atmospheric carbon. The regulatory mechanism(s) that control linear electron flow, known as “photosynthetic control,” are amplified in ...
Maureen Saint-Sorny, Pawel Brzezowski, Stéphanie Arrivault, Jean Alric, Xenie Johnson   +4 more
doaj   +1 more source

Mangrove plants using deoxyribonucleic acid barcodes for enhancing biodiversity and conservation [PDF]

Global Journal of Environmental Science and Management
BACKGROUND AND OBJECTIVES: Mangrove forests in North Sumatra and Aceh are concentrated on the east coast of Sumatra Island. Mangrove habitats are highly productive, diversified, and ecologically and commercially significant ecosystems.
M. Basyuni, R. Syahbana, A.B. Rangkuti, N.A. Pradisty, A. Susilowati, L.A.M. Siregar, S.S. Al Mustaniroh, A.A. Aznawi, A. Mubaraq, E.R. Ardli, S.H. Larekeng, V. Leopardas, Y. Isowa, T. Kajita   +13 more
doaj   +1 more source

Molecular mechanism of Rubisco activase: Dynamic assembly and Rubisco remodeling

Frontiers in Molecular Biosciences, 2023
Ribulose-1,5-bisphosphate (RuBP) carboxylase-oxygenase (Rubisco) enzyme is the limiting step of photosynthetic carbon fixation, and its activation is regulated by its co-evolved chaperone, Rubisco activase (Rca). Rca removes the intrinsic sugar phosphate
Kazi Waheeda, Kazi Waheeda, Heidi Kitchel, Heidi Kitchel, Quan Wang, Po-Lin Chiu, Po-Lin Chiu   +6 more
doaj   +1 more source

Protein transport in intact, purified pea etioplasts [PDF]

, 1986
We have developed a method to isolate intact, purified pea etioplasts. These etioplasts were capable of recognizing, transporting, and processing the precursor form of the small subunit of the ribulose-1,5-bisphosphate carboxylase, a protein which is not
Bonner, Chua, Cline, Coruzzi, Delepelaire, Douce, Fourcoy, Gallagher, Grossmann, Harpster, Jackson, Jenkins, Kannangara, Lütz, Maniatis, McCarthy, Mourioux, Pfisterer, Roberts, Sasaki, Smith, Soll, Soll, Thompson, Torriani   +24 more
core   +1 more source

Characterization of ribulose‐1,5‐bisphosphate carboxylase/oxygenase carrying ribulose 1,5‐bisphosphate at its regulatory sites and the mechanism of interaction of this form of the enzyme with ribulose‐1,5‐bisphosphate‐carboxylase/oxygenase activase [PDF]

European Journal of Biochemistry, 1992
Ribulose‐1,5‐bisphosphate carboxylase/oxygenase [Rbu(1,5)P2CO] from plant sources shows a biphasic reaction course when assayed with more than 2 mM ribulose 1,5‐bisphosphate [Rbu(1,5)P2]. In the burst, Rbu(1,5)P2CO has its substrate‐binding sites occupied with Rbu(1,5)P2 for the initial few minutes, then both substrate‐binding and regulatory sites are ...
Akiho Yokota, Noritaka Tsujimoto
openaire   +3 more sources

Crystal structure of activated ribulose-1,5-bisphosphate carboxylase complexed with its substrate, ribulose-1,5-bisphosphate

Journal of Biological Chemistry, 1991
The three-dimensional structure of the complex of ribulose-1,5-bisphosphate carboxylase from Rhodospirillum rubrum, CO2, Mg2+, and ribulose bisphosphate has been determined with x-ray crystallographic methods to 2.6-A resolution. Ribulose-1,5-bisphosphate binds across the active site with the two phosphate groups in the two phosphate binding sites of ...
T Lundqvist, Gunter Schneider
openaire   +3 more sources

Photosynthesis, Ribulose-1,5-bisphosphate Carboxylase, Electron Transport, and Ribulose 1,5-Bisphosphate of Virescent and Normal Green Wheat Leaves [PDF]

Plant Physiology, 1983
CO(2) gas exchange, ribulose-1,5-bisphosphate, and electron transport have been measured in leaves of a yellow-green mutant of wheat (Triticum durum var Cappelli) and its wild type strain grown in the field. All these parameters, expressed on leaf area basis, were similar in both genotypes except electron transport which was more than double in the ...
Liliana Tomarchio, Giorgio Dimarco, Lucio Triolo   +2 more
openaire   +3 more sources

Quantification of RuBisCO Expression and Photosynthetic Oxygen Evolution in Cyanobacteria

Bio-Protocol, 2021
Phototrophic microorganisms are frequently engineered to regulate the expression and the activity of targeted enzymes of interest for specific biotechnological and agricultural applications.
Mateusz Kędzior, Betul Kacar
doaj   +1 more source