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Glutathione redox potential in the mitochondrial intermembrane space is linked to the cytosol and impacts the Mia40 redox state
Author(s) -
Kojer Kerstin,
Bien Melanie,
Gangel Heike,
Morgan Bruce,
Dick Tobias P,
Riemer Jan
Publication year - 2012
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/emboj.2012.165
Subject(s) - mitochondrial intermembrane space , biology , redox , cytosol , intermembrane space , glutathione , mitochondrion , microbiology and biotechnology , biochemistry , biophysics , enzyme , escherichia coli , bacterial outer membrane , gene , materials science , metallurgy
Glutathione is an important mediator and regulator of cellular redox processes. Detailed knowledge of local glutathione redox potential (E GSH ) dynamics is critical to understand the network of redox processes and their influence on cellular function. Using dynamic oxidant recovery assays together with E GSH ‐specific fluorescent reporters, we investigate the glutathione pools of the cytosol, mitochondrial matrix and intermembrane space (IMS). We demonstrate that the glutathione pools of IMS and cytosol are dynamically interconnected via porins. In contrast, no appreciable communication was observed between the glutathione pools of the IMS and matrix. By modulating redox pathways in the cytosol and IMS, we find that the cytosolic glutathione reductase system is the major determinant of E GSH in the IMS, thus explaining a steady‐state E GSH in the IMS which is similar to the cytosol. Moreover, we show that the local E GSH contributes to the partially reduced redox state of the IMS oxidoreductase Mia40 in vivo . Taken together, we provide a comprehensive mechanistic picture of the IMS redox milieu and define the redox influences on Mia40 in living cells.