Proton nuclear magnetic resonance study of the binary complex of cytochrome P450cam and putidaredoxin: interaction and electron transfer rate analysis

FEBS Letters

Simonneaux, G.¹  De Certaines, J.D.⁵  Hui Bon Hoa, G.²  Spencer, R.G.S.³  Mouro, C.¹  Jung, C.⁴  Bondon, A.¹ 

[1] Laboratoire de Chimie Organométallique et Biologique, UMR CNRS 6509, Université de Rennes 1, Campus de Beaulieu, 35042 Rennes Cedex, France;Institut de Biologie Physico Chimique, Paris 75005, France;Nuclear Magnetic Resonance Unit, National Institute on Aging, National Institutes of Health, Baltimore, MD 21224, USA;Max Delbrück Center for Molecular Medicine, 13092 Berlin-Buch, Germany;Laboratoire de Résonance Magnétique en Biologie et Médicine, UPRES EA 2230, Université de Rennes 1, Campus de Villejean, 35043 Rennes Cedex, France

关键词: Cytochrome P450;    Putidaredoxin;    Electron transfer;    Nuclear magnetic resonance;    Isocyanide;   

DOI  :  10.1016/S0014-5793(99)00898-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A ¹H nuclear magnetic resonance study of the complex of cytochrome P450cam-putidaredoxin has been performed. Isocyanide is bound to cytochrome P450cam in order to increase the stability of the protein both in the reduced and the oxidized state. Diprotein complex formation was detected through variation of the heme methyl proton resonances which have been assigned in the two redox states. The electron transfer rate at equilibrium was determinated by magnetization transfer experiments. The observed rate of oxidation of reduced cytochrome P450 by the oxidized putidaredoxin is 27 (±7) per s.

【 授权许可】

Unknown