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in U.S.A. Cytochrome c1 has been purified from mitochondria of the yeast Saccharomyces cereoisiae. The procedure involves solubilization with cholate, ammonium sulfate fractionation, disruption of the cytochrome b.c, complex with mercaptoethanol and detergents, and chromatography on DEAE-cel- lulose.
Cytochrome c oxidase is the terminal complex of eukaryotic oxidative phosphorylation in mitochondria. This process couples the reduction of electron carriers during metabolism to the reduction of molecular oxygen to water and translocation of protons from the internal mitochondrial matrix to the inter-membrane space.
Cytochrome c is functionally involved in the electron transport chain of mitochondria. That electron transport is part of the pathway for synthesis of ATP. The role of cytochrome c is to carry electrons from one complex of integral membrane proteins of the inner mitochondrial membrane to another (Fig. 10.3).
Overexpression of cytochrome c enhances caspase activation and promotes cell death in response to apoptotic stimulation, but simple up-regulation of cytochrome c using an ecdysone-inducible system is, by itself, insufficient to induce apoptosis.
In particular, the oligomeric form of the pro-apoptotic protein Bax stimulates cytochrome c release, although the precise way in which this protein permeabilizes the outer mitochondrial membrane remains unclear. Cytochrome c is bound to the inner membrane by anionic phospholipids, primarily cardiolipin.
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Cytochrome c (Cyt c) shuttles electrons from oxidative phosphorylation complex III to complex IV. However, when it is released from mitochondria, it stimulates cell death (15) by interacting with Apaf-1 and recruiting and activating procaspase-9 (27, 46).

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