Structural and enzymological analysis of the interaction of isolated domains of cytochrome P‐450 BM3

FEBS Letters

Price, Nicholas C.¹  Coggins, John R.²  Lindsay, J.Gordon²  Munro, Andrew W.²  Kelly, Sharon M.¹ 

[1] Department of Biological and Molecular Sciences, University of Stirling, Stirling, FK94LA, UK;Department of Biochemistry, University of Glasgow, Glasgow, G12 8QQ, UK

关键词: Cytochrome P-450 BM3;    Domain interaction;    Circular dichroism;    Electron transfer;    Haem environment;    P-450;    cytochrome P-450 linked monooxygenase;    IPTG;    isopropyl-β-d-thio-galactopyranoside;    MOPS;    morpholinopropane-sulphate;    FAD;    flavin adenine dinucleotide;    FMN;    flavin mononucleotide;    CO;    carbon monoxide;    NO;    nitric oxide;    CD;    circular dichroism;    EPR;    electron paramagnetic resonance;    UV;    ultra violet;   

DOI  :  10.1016/0014-5793(94)80609-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The interactions of the individually expressed haem- and flavin-containing domains of cytochrome P-450 BM3 have been analysed by enzymological and spectroscopic techniques. Electron transfer between the isolated domains occurs at a much lower rate than that occurring in the intact flavocytochrome. CD spectroscopic studies indicate that the linkage of the domains in intact P-450 BM3 creates haem and amino acid environments suitable for efficient electron transfer from its flavin domain.

【 授权许可】

Unknown