RuBisCO-RuBP complex. Computer model showing the active site of a molecule of the carbon fixation enzyme ribulose-1,5-bisphosphate carboxylase oxygena
RuBisCO-RuBP complex. Computer model showing the active site of a molecule of the carbon fixation enzyme ribulose-1,5-bisphosphate carboxylase oxygenase (RuBisCO), from a spinach plant (Spinacia oleracea), in complex with a molecule of its natural substrate ribulose 1,5-bisphosphate (RuBP, red) in its transition state, and a Mg2+ magnesium ion (green). RuBisCO is an enzyme that aids carbon fixation - the conversion of inorganic carbon from forms such as carbon dioxide to organic compounds by living organisms in processes such as photosynthesis. It is a hexadecamer composed of 8 heavy catalytic subunits (blue and white ribbons) and 8 light regulatory subunits (yellow and orange). The Mg2+ ion is critical for the process of fixing carbon from carbon dioxide.
Size: 4048px × 4500px
Photo credit: © RAMON ANDRADE 3DCIENCIA/SCIENCE PHOTO LIBRARY / Alamy / Afripics
License: Licensed
Model Released: No
Keywords: 1, 5-biphosphate, 5-bisphosphate, artwork, atom, background, biochemical, biochemistry, biological, biology, biomolecule, carbon, carboxylase/oxygenase, catalyst, catalytic, cell, cellular, complex, complexed, conversion, converting, cut, cut-, cut-outs, cutout, cutouts, enzyme, enzymes, fixation, hexadecamer, illustration, ion, magnesium, mg2, model, molecular, molecules, oleracea, organic, outs, photosynthesis, photosynthetic, protein, proteins, proteomics, quaternary, regulatory, ribulose, ribulose-1, rubisco, rubp, secondary, spinach, spinacia, structural, structure, structures, substrate, subunit, subunits, white
