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  • Title: A spectrometric study of the Co(2+)-activated ribulose-1,5-bisphosphate carboxylase reaction during turnover and at different pH.
    Author: Janson K, Brändén R.
    Journal: Biochim Biophys Acta; 1991 Oct 11; 1080(1):40-4. PubMed ID: 1657177.
    Abstract:
    EPR as well as optical absorption studies of the Co(2+)-activated ribulose-1,5-bisphosphate carboxylase/oxygenase under turnover conditions show that the formation of the two detectable intermediates are pH dependent. The amount of one of them, which earlier has been proposed to be a metal coordinated endiol of ribulose-1,5-bisphosphate (Brändén et al. (1987) Biochim. Biophys. Acta 916, 298-303), increased with increasing pH. Distinct optical absorption bands could be assigned to this intermediate and a pH profile could be made. It is therefore proposed that a base with a pKa value of about 8 is responsible for the enzyme-catalysed abstraction of a proton from ribulose-1,5-bisphosphate in order to form the metal coordinated endiol of ribulose-1,5-bisphosphate.
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