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Inhibition of ribulose-1,5-bisphosphate carboxylase-oxygenase activities by hydroxylamine

Biochimica et Biophysica Acta (BBA) - Enzymology, 1980
Hydroxylamine directly and reversibly inhibits both activities of homogeneous ribulose-1,5-bisphosphate carboxylase-oxygenase (3-phospho-D-glycerate carboxy-lyase (dimerizing), EC 4.1.1.39) isolated from diverse sources. NH2OH is an uncompetitive inhibitor of carboxylase activity with respect to ribulose-bisphosph ate.
Hugh M. Brown   +2 more
openaire   +3 more sources

Electrostatic fields at the active site of ribulose‐1,5‐bisphosphate carboxylase

Proteins: Structure, Function, and Bioinformatics, 1992
AbstractA macroscopic approach has been employed to calculate the electrostatic potential field of nonactivated ribulose‐1,5‐bis‐phosphate carboxylase and of some complexes of the enzyme with activator and substrate. The overall electrostatic field of the L2‐type enzyme from the photosynthetic bacterium Rhodospirillum rubrum shows that the core of the ...
Ylva Lindqvist   +2 more
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d-ribulose-1,5-bisphosphate carboxylase in Chlorobium thiosulfatophilum Tassajara

Biochimica et Biophysica Acta (BBA) - Enzymology, 1974
Abstract d -Ribulose-1,5-bisphosphate carboxylase (3-phospho- d -glycerate carboxy-lyase (dimerizing), EC 4.1.1.39) was readily detected in extracts of Chlorobium thiosulfatophilium Tassajara after transatlantic air delivery. The enzyme, which was moderately unstable, had a specific activity of 7 nmoles CO 2 fixed/min per mg protein when assayed ...
Bruce A. McFadden   +5 more
openaire   +3 more sources

Large structures at high resolution: the 1.6 A crystal structure of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase complexed with 2-carboxyarabinitol bisphosphate.

Journal of Molecular Biology, 1996
Ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) from spinach is a hexadecamer (L8S8, Mr = 550,000) consisting of eight large (L, 475 residues) and eight small subunits (S, 123 residues).
Inger Andersson
semanticscholar   +1 more source

Subunit arrangement of spinach ribulose 1,5-bisphosphate carboxylase/oxygenase

Planta, 1985
The structure of spinach ribulose 1,5-bisphosphate carboxylase/oxygenase (EC 4.1.1.39) has been investigated by tilted-view electron microscopy of negatively stained monolayer crystals and image processing. The structure determined consists of a cylinder of octagonal cross-section with a large central hole.
J. A. Barcena, Peter Shaw
openaire   +3 more sources

[9] Activation and assay of ribulose-1,5-bisphosphate car☐ylase/oxygenase

1982
Publisher Summary This chapter describes the activation and assay of ribulose-l,5-bisphosphate (ribulose-P 2 ) carboxylase–oxygenase. It is a bifunctional enzyme that catalyzes the addition of CO 2 or O 2 to C-2 of ribulose-P 2 . The products of the carboxylase reaction are two molecules of D-glycerate-3-P and the enzyme activity is systematically ...
Mulligan Rm   +3 more
openaire   +3 more sources

Isolation of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase from Leaves

2010
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is a multifunctional enzyme that catalyzes the fixation of CO2 and O2 in photosynthesis and photorespiration, respectively. As the rate-limiting step in photosynthesis, improving the catalytic properties of Rubisco has long been viewed as a viable strategy for increasing plant productivity ...
Carmo-Silva, A. Elizabete   +2 more
openaire   +3 more sources

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