Structural diversity of cytochrome P450 enzyme system

Abstract

Cytochrome P450 enzyme system consists of P450 and its NAD(P)H-linked reductase or reducing system, and catalyses monooxygenation reactions. The most prevalent type in eukaryotic organisms is 'microsomes type', which consists of membrane-bound P450 and NADPH-P450 reductase. The second type is 'mitochondria type', in which P450 is bound to the inner membrane while the reducing system consisting of an NADPH-linked flavoprotein and a ferredoxin-type iron-sulphur protein is soluble in the matrix space. The third type is 'bacteria type', in which both P450 and the reducing system are soluble in the cytoplasm. In addition to these three types, several forms of P450-reductase fusion proteins have been found in prokaryotic organisms. On the other hand, some P450s catalyse the re-arrangement of the oxygen atoms in the substrate molecules that does not require the supply of reducing equivalents for the reaction. A peculiar P450, P450nor, receives electrons directly from NADH for the reduction of nitric oxide.