NMR studies of binding of 5-FdUDP and dCDP to ribonucleoside-diphosphate reductase from Escherichia coli
作者： Béatrice Roy , Jean-Luc Decout , Claude Béguin , Marc Fontecave , Peter Allard
DOI: 10.1016/0167-4838(94)00241-8
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摘要: Abstract 5-Fluoro-2′-deoxyuridine-5′-diphosphate (5-FdUDP) has been synthesised using an original route, previously applied to the synthesis of natural nucleoside diphosphates. The interaction between 5-FdUDP and enzyme ribonucleoside-diphosphate reductase (EC 1.17.4.1) studied with t9F-NMR. product analogue is shown be in fast exchange substrate. binding sites on protein subunit 1 (R1) (NDP) reductase. number reduced alf when complete holoenzyme R1R2 formed. temperature dependence line broadening was 19F-NMR, dCDP dUDP 1H-NMR. dependences are complex a molecular model which R1 dependent equilibrium at least two conformations suggested order explain observed behaviour. Binding ligand substrate affects conformational specific way. Formation also equilibrium.
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