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

TL;DR

This study uncovers a novel cascade of reactions involving serum albumin, where p-nitrophenyl acetate is transformed into p-nitrophenol and further reacts via radical formation, influenced by infrared light, revealing new biochemical roles.

Contribution

It demonstrates that serum albumin catalyzes a complex reaction cascade involving radical formation and proton coupled electron transfer, extending beyond traditional esterase activity, and shows infrared light can modulate this process.

Findings

Serum albumin catalyzes a reaction cascade involving radical formation.

Infrared light influences the proton coupled electron transfer process.

p-Nitrophenol undergoes further transformation with HNO2 release.

Abstract

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