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Hexokinase inhibits flux of fluorescently labeled ATP through mitochondrial outer membrane porin
Author(s) -
Perevoshchikova Irina V.,
Zorov Savva D.,
Kotova Elena A.,
Zorov Dmitry B.,
Antonenko Yuri N.
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.04.033
Subject(s) - voltage dependent anion channel , hexokinase , bodipy , mitochondrion , atp–adp translocase , biochemistry , bacterial outer membrane , porin , adenosine triphosphate , biophysics , organelle , inner mitochondrial membrane , chemistry , microbiology and biotechnology , biology , fluorescence , glycolysis , metabolism , physics , escherichia coli , quantum mechanics , gene
Mitochondrial function requires maintaining metabolite fluxes across the mitochondrial outer membrane, which is mediated primarily by the voltage dependent anion channel (VDAC). We applied fluorescence correlation spectroscopy (FCS) to study regulation of the VDAC functional state by monitoring distribution of fluorescently labeled ATP (BODIPY‐FL‐ATP) in isolated intact rat liver and heart mitochondria. Addition of mitochondria to BODIPY‐FL‐ATP solution resulted in accumulation of the fluorescent probe in these organelles. The addition of hexokinase II (HKII) isolated from rat heart led to a decrease in the BODIPY‐FL‐ATP accumulation, while a 15‐residue peptide corresponding to the N‐terminal domain of hexokinase did not produce this effect. Therefore, the hexokinase‐induced inhibition of the ATP flow mediated by VDAC was revealed in isolated mitochondria.