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.