Evaluation of the Functional Role of the Heme-6-propionate Side Chain in Cytochrome P450cam

摘要

The heme b (protoheme Ⅸ) prosthetic group binds to the protein matrix of hemoproteins via multiple noncovalent interactions to form a holoprotein, in which two peripheral heme-propionates have been generally regarded as functioning as anchors for the heme group by forming interactions with the generally polar protein matrix. In the case of the cytochrome P450cam (P450cam), the monooxygenase responsible for d-camphor hydroxylation, the heme-6-propionate side chain forms hydrogen bonds with Thrl101, Gln 108, Arg112, and His355.