1H-NMR study of diamagnetic cytochrome P450cam: assignment of heme resonances and substrate dependance of one cysteinate beta proton.
The 1H-NMR study of diamagnetic cytochrome P450cam FeII-CO has been performed for the first time. Chemical shifts of the cysteinate fifth ligand protons and of several heme protons have been assigned through 1- and 2-dimensional spectra at 500 MHz. A substrate dependance has been observed for the resonance of the cysteinate proton detected in the high-field region.
Mouro
C
C
Laboratoire de Chimie Organométallique et Biologique, UMR CNRS 6509, Université de Rennes 1, Campus de Beaulieu, France.
Bondon
A
A
Simonneaux
G
G
Jung
C
C
D001665:Binding Sites; D019475:Camphor 5-Monooxygenase / Q000737:chemistry* / Q000378:metabolism*; D002248:Carbon Monoxide; D003545:Cysteine; D006418:Heme / Q000032:analysis*; D006859:Hydrogen; D007501:Iron; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008280:Magnetics; D008958:Models, Molecular; D010084:Oxidation-Reduction; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity
D011994:Recombinant Proteins; D006418:Heme; D002248:Carbon Monoxide; D006859:Hydrogen; D007501:Iron; D019475:Camphor 5-Monooxygenase; D003545:Cysteine