Photoinduced electron transfer from a novel nanotrigger addressed to the NADPH site within the endothelial NO-synthase to the flavin moieties of the protein

Abstract : We developed a new selective molecular tool to trigger enzymatic activity in a synchronous manner and monitor the sequence of the kinetic events by ultra-fast transient spectroscopy. Our approach is based on a synthetic nanotrigger addressing a selected site within proteins, namely the conserved NADPH binding site common to many enzymes involved in bioreductive processes [1]. The nanotrigger combines a "docking" subunit responsible for the recognition of NADPH sites within proteins and a "chromophoric" subunit responsive to light excitation and able to transfer electrons to the flavin moieties of proteins. We present the first spectroscopic data on such a nanotrigger [1] in the presence of the reductase domain of the endothelial nitric oxide synthase eNOSred.
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Edward Beaumont, Anne-Claire Robin, Vladimir Berka, Ah-Lim Tsai, Mireille Blanchard-Desce, et al.. Photoinduced electron transfer from a novel nanotrigger addressed to the NADPH site within the endothelial NO-synthase to the flavin moieties of the protein. Nitric Oxide: Biology and Chemistry, Elsevier, 2006, 14 (4), pp.14-15. ⟨10.1016/j.niox.2006.04.050⟩. ⟨hal-00844508⟩

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