Assignment of heme methyl 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.
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. & 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.
Mouro
C
C
Laboratoire de Chimie Organométallique et Biologique, UMR CNRS 6509, Université de Rennes 1, Campus de Beaulieu, France.
Bondon
A
A
Jung
C
C
De Certaines
J D
JD
Simonneaux
G
G
D002164:Camphor / Q000378:metabolism; D019475:Camphor 5-Monooxygenase / Q000737:chemistry* / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy; D005288:Ferredoxins / Q000378:metabolism; D005290:Ferric Compounds / Q000378:metabolism*; D006418:Heme / Q000737:chemistry* / Q000378:metabolism*; D008024:Ligands; D009570:Nitriles / Q000378:metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular; D011522:Protons
D005288:Ferredoxins; D005290:Ferric Compounds; D008024:Ligands; D009570:Nitriles; D011522:Protons; C002990:butyl isocyanide; D006418:Heme; C100137:putidaredoxin; C001187:ethyl isocyanide; D002164:Camphor; D019475:Camphor 5-Monooxygenase