Energy transfer from tryptophan residues to pyridoxal 5'-phosphate at the active site of ribulose-1,5-bisphosphate carboxylase/oxygenase.
Forster's mechanism of radiationless energy transfer has been used to estimate average distance between tryptophan residues and pyridoxal 5'-phosphate bound at the active site of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase. This distance was found to depend on the activity of the enzyme and was 29 A for a freshly purified enzyme (activity 1.7 mu moles CO2 fixed/min/mg protein) and 37 A for a 6 week old enzyme stored at 4 degrees C (activity 0.07 mu moles CO2 fixed/min/mg protein).
D001665:Binding Sites; D008433:Mathematics; D010944:Plants / Q000201:enzymology; D011732:Pyridoxal Phosphate / Q000378:metabolism*; D012273:Ribulose-Bisphosphate Carboxylase / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D014364:Tryptophan / Q000378:metabolism*
D011732:Pyridoxal Phosphate; D014364:Tryptophan; D012273:Ribulose-Bisphosphate Carboxylase