Substrate interactions in cytochrome P-450: correlation between carbon-13 nuclear magnetic resonance chemical shifts and C-O vibrational frequencies.
13CO NMR chemical shifts and 12CO infrared stretching frequencies have been measured for cytochrome P-450cam-CO in the presence of D-camphor and of various camphor analogues. A linear correlation between both parameters delta (13C) and v(CO) was found indicating that the steric and electrostatic interactions acting on the CO ligand are influenced by the substrate. It has been proved that P-450 complexes are on another line in this correlation than hemoglobins which is explained by the different proximal ligand.
Legrand
N
N
Laboratoire de Chimie Organométallique et Biologique, URA CNRS 415, Université de Rennes 1, France.
Bondon
A
A
Simonneaux
G
G
Jung
C
C
Gill
E
E
D002164:Camphor / Q000031:analogs & derivatives; D019475:Camphor 5-Monooxygenase; D002247:Carbon Isotopes; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D004563:Electrochemistry; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D006899:Mixed Function Oxygenases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D017550:Spectroscopy, Fourier Transform Infrared; D013379:Substrate Specificity
D002247:Carbon Isotopes; D008024:Ligands; D002164:Camphor; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; D019475:Camphor 5-Monooxygenase