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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
Author(s) -
Kowacz Magdalena,
Warszyński Piotr
Publication year - 2019
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.2780
Subject(s) - chemistry , bovine serum albumin , imidazole , histidine , photochemistry , esterase , phenol , serum albumin , hydrolysis , electron transfer , nitro , organic chemistry , enzyme , biochemistry , alkyl
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 HNO 2 . 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.