Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

Part I. An investigation of the substrate and ligand binding sites of the cytochrome P-450-CAM using nuclear magnetic resonance spectroscopy. Part II. A nuclear magnetic resonance study of (1R)-(+)-camphor and twenty-five camphor derivatives using one- and two-dimensional methods

Thesis/Dissertation ·
OSTI ID:6411704

The distance between the heme iron of ferrous cytochrome P-450-CAM and a fluorine label attached to the 9-methyl group of its substrate, (1R)-(+)-camphor, has been determined using /sup 19/F NMR. This investigation is the first use of the Solomon-Bloembergen equation to determine the distance from a substrate-bound fluorine that is not in fast exchange to a paramagnetic heme iron. The paramagnetic relaxation rate data and the correlation time have been used to calculate a distance of 3.8 A between the heme iron and the C-9 fluorine. The interaction of fluoride ion with the ferric high-spin heme iron of cytochrome P-450-CAM and of myoglobin has also been investigated using /sup 19/F NMR relaxation measurements. The carbon, proton, and deuterium NMR properties of (1R)-(+)-camphor have been thoroughly investigated by both one- and two-dimensional procedures. This has allowed the first definitive assignments of the resonances of all of the carbons and protons in camphor to be made. The NMR spectra of twenty-five camphor derivatives have been examined by one- and two-dimensional methods and the resonances assigned.

Research Organization:
South Carolina Univ., Columbia (USA)
OSTI ID:
6411704
Country of Publication:
United States
Language:
English