Conference paper

The Structure and Mechanism of Cytochrome P450

V. Ullrich ; Department of Physiological Chemistry, University of the Saarland, D - 665 Homburg-Saar, FRG
H. H. Ruf ; Department of Physiological Chemistry, University of the Saarland, D - 665 Homburg-Saar, FRG
P. Wende ; Department of Physiological Chemistry, University of the Saarland, D - 665 Homburg-Saar, FRG

Abstract

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.

Keywords

Hrčak ID:

196361

URI

https://hrcak.srce.hr/196361

Publication date:

30.3.1977.

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