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Assignment of heme methyl 1 H‐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

2000; Wiley; Volume: 267; Issue: 1 Linguagem: Inglês

10.1046/j.1432-1327.2000.00995.x

1432-1033

Corinne Rondeau‐Mouro, Arnaud Bondon, Christiane Jung, Jacques D. de Certaines, Gérard Simonneaux,

Advanced NMR Techniques and Applications

An 1 H‐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. & 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.