Substrate interactions in cytochrome P-450: correlation between carbon-13 nuclear magnetic resonance chemical shifts and C-O vibrational frequencies

• Published in: FEBS letters Vol. 364; no. 2; pp. 152 - 156
• Main Authors: Legrand, N., Bondon, A., Simonneaux, G., Jung, C., Gill, E.
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 08.05.1995
• Subjects: 13C NMR; Camphor - analogs & derivatives; Camphor 5-Monooxygenase; Carbon Isotopes; Cytochrome P-450; Cytochrome P-450 Enzyme System - chemistry; Cytochrome P-450 Enzyme System - genetics; Cytochrome P-450 Enzyme System - metabolism; Electrochemistry; Escherichia coli - enzymology; Escherichia coli - genetics; FT-IR; Ligands; Magnetic Resonance Spectroscopy; Mixed Function Oxygenases - chemistry; Mixed Function Oxygenases - genetics; Mixed Function Oxygenases - metabolism; Spectroscopy, Fourier Transform Infrared; Substrate interaction; Substrate Specificity; FT-IR; Substrate interaction; 13C NMR; Cytochrome P-450
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(95)00377-L

13CO NMR chemical shifts and 12CO infrared stretching frequencies have been measured for cytochrome P-450camCO in the presence of d-camphor and of various camphor analogues. A linear correlation between both parametersδ( 13C and ν(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.