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
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
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Related Subjects
59 BASIC BIOLOGICAL SCIENCES
BARYONS
CAMPHOR
CYTOCHROMES
ELEMENTARY PARTICLES
EQUATIONS
FERMIONS
FLUORINE 19
FLUORINE ISOTOPES
HADRONS
ISOTOPE APPLICATIONS
ISOTOPES
KETONES
LIGANDS
LIGHT NUCLEI
MAGNETIC RESONANCE
MEMBRANE PROTEINS
MOLECULAR STRUCTURE
NMR SPECTRA
NUCLEAR MAGNETIC RESONANCE
NUCLEI
NUCLEONS
ODD-EVEN NUCLEI
ORGANIC COMPOUNDS
PIGMENTS
PROTEINS
PROTONS
RECEPTORS
RESONANCE
SPECTRA
STABLE ISOTOPES
SUBSTRATES
TERPENES
TRACER TECHNIQUES