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

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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., Bondon, A., Jung, C., 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
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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