Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture. Binds to eukaryotic membranes where it hydrolyzes phosphatidylcholine. This enzyme has 10-fold less activity towards sphingomyelin than its C.perfringens counterpart, is approximately 100-fold less hemolytic against mouse erythrocytes and at least 100-fold less toxic in mice. a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-sn-glycerol + H(+) + phosphocholine Binds 3 Ca(2+) ions per subunit. Binds 3 Zn(2+) ions per subunit. The protein is composed of 2 domains; the N-terminal domain contains the phospholipase C active site (PLC), in a cleft which is also occupied by the 3 zinc ions. The C-terminal domain is a putative phospholipid-recognition domain, which shows structural homology with phospholipid-binding C2-like domains from a range of eukaryotic proteins. The ability to bind membrane phospholipids in a Ca(2+) dependent manner is conferred by this C-terminal domain (By similarity). A hybrid protein between the N-terminus of C.bifermentans and the C-terminus of C.perfringens has an activity intermediate between the two. Belongs to the bacterial zinc-metallophospholipase C family.