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Assignment of heme mythyl 1H-NMR resonances of high-spin and low-spin ferric complexes of cytochrome P450cam using one-dimensional and two-dimensional paramagnetic signals enhancement (PASE) magnetization transfer experiments

Item Type:Article
Title:Assignment of heme mythyl 1H-NMR resonances of high-spin and low-spin ferric complexes of cytochrome P450cam using one-dimensional and two-dimensional paramagnetic signals enhancement (PASE) magnetization transfer experiments
Creators Name:Mouro, C. and Bondon, A. and Jung, C. and De Certaines, J.D. and Simonneaux, A.
Abstract:An 1H-NMR study of ferric cytochrome P450cam in different paramagnetic states was performed. Assignment of three heme methyl resonances of the isocyanide adduct of cytochrome P450 in the ferric low-spin state was recently performed using electron exchange in the presence of putidaredoxin [Mouro, C., Bondon, A., Jung, C., Hui Bon Hoa, G., De Certaines, J.D., Spencer, R.G.S. and Simonneaux, G. (1999) FEBS Lett. 455, 302-306]. In this study, heme methyl protons of cytochrome P450 in the native high-spin and low-spin states were assigned through one-dimensional and two-dimensional magnetization transfer spectroscopy using the paramagnetic signals enhancement (PASE) method. The order of the methyl proton chemical shifts is inverted between high-spin and low-spin states. The methyl order observed in the ferric low-spin isocyanide complexes is related to the orientation of the cysteinate ligand.
Keywords:Cytochrome P450, Isocyanides, NMR, Paramagnetic
Source:European Journal of Biochemistry
ISSN:0014-2956
Publisher:Blackwell Publishing (U.K.)
Volume:267
Number:1
Page Range:216-221
Date:1 January 2000
Official Publication:https://doi.org/10.1046/j.1432-1327.2000.00995.x
PubMed:View item in PubMed

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