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Serum albumin, recognized mainly for its capacity to act as a carrier proteinfor many compounds, can also actively transform some organic molecules. As astarting point in this study we consider esterase-like activity of bovine serumalbumin (BSA) toward p-nitrophenyl acetate (p-NPA). Our results reveal that thereaction goes beyond ester hydrolysis step. In fact the transformation product,p-nitrophenol (p-NP), becomes a substrate for further reaction with BSA inwhich its nitro group in subtracted and released in the form of HNO2. Spectraldata indicate that this cascade of events proceeds through formation ofphenoxyl radical via proton coupled electron transport (PCET) between OH groupof p-NP and imidazole ring of histidine from the protein. Furthermore, theeffect of application of electromagnetic radiation in the infrared range,suggests that this remote physical trigger can support interactions based onPCET mechanism by acting on polarization and mutual alignment of water dipolesserving as effective water wires.

Beyond esterase-like activity of serum albumin. Histidine-(nitro)phenol  radical formation in conversion cascade of p-nitrophenyl acetate and the role  of infrared light