The oxidation of naphthalene and pyrene by cytochrome P450cam

FEBS Letters

England, Paul A¹  Wong, Luet-Lok¹  Stevenson, Julie-Anne¹  Harford-Cross, Charles F¹  Rouch, Duncan A¹ 

[1] Department of Chemistry, Inorganic Chemistry Laboratory, South Parks Road, Oxford OX1 3QR, UK

关键词: P450cam;    Monooxygenase;    Mutagenesis;    Protein engineering;    Polycyclic aromatic hydrocarbon;   

DOI  :  10.1016/S0014-5793(98)00189-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Mutants of the heme monooxygenase cytochrome P450_cam in which Y96 had been replaced with hydrophobic residues, have been shown to oxidise naphthalene and pyrene with rates one to two orders of magnitude faster than the wild-type. Naphthalene was oxidised to 1- and 2-naphthol, probably via the 1,2-oxide intermediate. In the case of the Y96F mutant, naphthalene was oxidised at a rate comparable to camphor. Pyrene oxidation gave 1,6- and 1,8-pyrenequinone with no evidence for attack at the K-region, in contrast to mammalian enzymes. The results show that the Y96 residue plays a key role in controlling the substrate range of P450_cam.

【 授权许可】

Unknown