Claim · model-written summary
Labeled cyanide bound to carboxylase only with ribulose diphosphate.
Not reportedTaxonMaterialGeneCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleTreatmentComparatorSettingDirectionQualifier
Verbatim
e0“14C-cyanide is bound to the carboxylase (1.06 moles of cyanide per mole of enzyme) only in the presence of ribulose-1,5-di-P”
Title
Inhibition of Ribulose Diphosphate Carboxylase by Cyanide
M Wishnick; M D Lane Journal of Biological Chemistry 1969. doi:10.1016/s0021-9258(19)78190-3
Other claims from this paper (8)
- Intervention effect Cyanide reversibly inhibited spinach leaf carboxylase by 51% at 10-5 m.
- Intervention effect Cyanide inhibited carboxylation by 91% at 10-4 m.
- Observation Cyanide inhibition was uncompetitive with ribulose diphosphate and mixed with Mg2+ and HCO3-.
- Mechanism Binding studies supported formation of an inactive enzyme–substrate–cyanide complex.
- Observation Labeled ribulose diphosphate bound tightly to carboxylase only with cyanide.
- Observation Mg2+ did not affect either labeled ligand binding measurement.
- Observation The enzyme, substrate and cyanide formed a 1:1:1 ternary complex.
- Observation Schiff base formation could not be demonstrated.