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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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