Final answer:
The mitochondrial complex driving apoptosis is initiated by cytochrome C release, which forms a complex that activates procaspases into caspases, the enzymes that digest cellular proteins leading to cell death.
Step-by-step explanation:
The complex found in the mitochondria that drives apoptosis is initiated by the release of cytochrome C into the cytoplasm. Cytochrome C, a peripheral membrane protein, exists in equilibrium between the membrane-bound and unbound states within the cristae. Upon release, it binds to adaptor proteins, forming a complex which has a high affinity for procaspases. The subsequent binding of procaspase to the cytochrome C-adaptor complex triggers an allosteric change, activating the procaspase into an active caspase. These active caspases are crucial proteolytic enzymes that initiate the digestion of cellular proteins, leading to the systematic auto-digestion of the cell. Additionally, Bcl2 proteins Bak and Bax are involved as they form outer mitochondrial membrane channels that release cytochrome C in response to apoptotic signals. It is important to note that caspace-dependent and -independent pathways can lead to mitochondrial damage during apoptosis, as evidenced by research cited from various journals.