Open AccessNAD(P)H: FMN-oxidoreductase functioning under macromolecular crowding: in vitro modeling
Author(s) -
A. E. Govorun,
Ele. Esimbekova,
Valentina A. Kratasyuk
Publication year - 2019
Publication title -
doklady akademii nauk. rossijskaâ akademiâ nauk
Language(s) - English
Resource type - Journals
ISSN - 0869-5652
DOI - 10.31857/s0869-56524864500-503
Subject(s) - oxidoreductase , nad+ kinase , in vitro , macromolecule , dissociation (chemistry) , macromolecular crowding , chemistry , dissociation constant , enzyme , biochemistry , biophysics , biology , receptor
The functioning of Vibrio fischeri NAD(P)H: FMN-oxidoreductase (Red) under conditions of macromolecular crowding (MMC) modeled in vitro by adding biopolymers (starch and gelatin) was studied. The dissociation rate constants and the activation energies of dissociation of Red to the subunits were calculated; the process of denaturation of Red was analyzed. It was shown that the functioning of Red both under conditions of MMC and diluted solutions is the same. The result refutes the common belief that due to MMC the stabilization of enzymes’ native conformation occurs in vivo when compared to in vitro.