Premium
An investigation of ribulosebisphosphate carboxylase activity by high resolution 1 H NMR
Author(s) -
Gutteridge Steven,
Parry Martin A.J.,
Schmidt C.N.Godfrey,
Feeney Jim
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)81343-5
Subject(s) - chemistry , deuterium , pyruvate carboxylase , ribulose , oxygenase , rubisco , phosphoglycerate kinase , substrate (aquarium) , nuclear magnetic resonance spectroscopy , molecule , stereochemistry , enzyme , biochemistry , organic chemistry , physics , quantum mechanics , oceanography , geology
The reactions catalysed by ribulosebisphosphate carboxylase/oxygenase have been studied by high resolution proton NMR spectroscopy. The protons of the substrate ribulose‐P 2 and the products of the carboxylase and oxygenase reactions are readily assigned to the various carbon centres. Half of the 3‐phosphoglycerate molecules generated during carboxylase turnover of ribulose‐P 2 in saturating CO 2 concentrations acquire deuterium from the solution at the C 2 position, whereas the other 3‐phosphoglycerate molecules and also the 3‐phosphoglycerate produced as a result of the oxygenase activity contain no deuterium of this type. However, the addition of activated enzyme (i.e., in the presence of an effector) to a solution of ribulose‐P 2 in the near absence of either CO 2 or O 2 catalyses the exchange of the C 3 proton with the deuterium of the solution.