%0 Journal Article
%T The Structure and Mechanism of Cytochrome P450
%A Ruf
%A H. H.
%A Ullrich
%A V.
%A Wende
%A P.
%J -
%D 1977
%X Sa£¿etak The unusual hemoprotein called cytochrome P450 is now recognized as representing a variety of monooxygenases with entirely different substrate specificities. In comparison with hememercaptide models it can be concluded that the unusual spectral properties reside in a heme-mercaptide linkage to the protein. The sixth ligand in the ferric form could be a hydroxyl group which is absent in the enzyme-substrate complex. In the reaction cycle the enzyme-substrate complex is reduced and then reacts with dioxygen to form an oxy-complex. Further reduction is believed to yield an £¿oxenoid£¿ complex of the structure [Fe0]3+, which transfers the oxygen atom to the substrate
%U https://hrcak.srce.hr/index.php?show=clanak&id_clanak_jezik=289476