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Apoptosis is triggered by an accumulation of ROS (reactive oxygen species) produced by proteins of the mitochondrial respiratory chain. The levels of ROS are controlled by the activities of mitochondrial redox proteins such as glutaredoxin 2 that help to modulate the susceptibility of a cell to apoptosis. However, once downstream events have resulted in the release of cytochrome c to the cytosol, it is widely considered that cell death is inevitable. Cytochrome c may promote its own release from mitochondria through interactions with the mitochondrial phospholipid cardiolipin (diphosphatidylglycerol). In the present article, spectroelectrochemistry of the cardiolipin complex of cytochrome c and protein film electrochemistry of glutaredoxin 2 are reviewed to illustrate how electrochemical methods provide insight into the properties of signalling proteins.
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