Cytochrome C (Saccharomyces cerevisiae)

Cytochrome C (Saccharomyces cerevisiae) exhibits a significant enhancement in the enzymatic activity of yeast chain-like complex IV (CIV) when it is modified with phosphorylation mimetic. This indicates that its activity can be regulated by its own phosphorylation status, and this phosphorylation-dependent regulatory function requires the participation of the respiratory supercomplex factor 1 (Rcf1) of the hypoxia-inducible gene domain (HIGD) protein family^[2].
Cytochrome C (Saccharomyces cerevisiae) is released from the intermembrane space of the mitochondria into the cytoplasm when the cell receives an apoptotic signal. In the cytoplasm, it no longer performs its normal respiratory function but instead acts as a crucial apoptotic signaling molecule, binding to apoptotic protease activating factor-1 (APAF-1), initiating the caspase cascade reaction, and ultimately leading to cell apoptosis^[3].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.