Open AccessAssignment 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
Author(s) -
Mouro Corinne,
Bondon Arnaud,
Jung Christiane,
De Certaines Jacques D.,
Simonneaux Gérard
Publication year - 2000
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.1432-1327.2000.00995.x
Subject(s) - chemistry , ferric , paramagnetism , spin states , magnetization , adduct , spin (aerodynamics) , heme , crystallography , hemeprotein , cytochrome , ligand (biochemistry) , nuclear magnetic resonance , inorganic chemistry , condensed matter physics , physics , organic chemistry , magnetic field , biochemistry , receptor , quantum mechanics , thermodynamics , enzyme
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.