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An investigation of ribulosebisphosphate carboxylase activity by high resolution 1H NMR

Research output: Contribution to Journal/MagazineJournal articlepeer-review

<mark>Journal publication date</mark>21/05/1984
<mark>Journal</mark>FEBS Letters
Issue number2
Number of pages5
Pages (from-to)355-359
Publication StatusPublished
<mark>Original language</mark>English


The reactions catalysed by ribulosebisphosphate carboxylase/oxygenase have been studied by high resolution proton NMR spectroscopy. The protons of the substrate ribulose-P2 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-P2 in saturating CO2 concentrations acquire deuterium from the solution at the C2 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-P2 in the near absence of either CO2 or O2 catalyses the exchange of the C3 proton with the deuterium of the solution.