Fourier transform phosphorus magnetic resonance study of the interaction of P-enolpyruvate with the muscle pyruvate kinase-gadolinium complex

Journal Article · Mon Jun 02 00:00:00 EDT 1975 · Biochem. Biophys. Res. Commun.; (United States)

DOI:https://doi.org/10.1016/0006-291X(75)90117-5· OSTI ID:7276087

Cottam, G L ^[1]; Ward, R L

---

1. Univ. of Texas, Dallas

The phosphorus spin-lattice relaxation rates of P-enolpyruvate is enhanced 13 fold in the presence of muscle pyruvate kinase and gadolinium as compared to either enzyme or metal ion alone. In the presence of the enzyme-gadolinium complex the phosphorous relaxation rate decreases as the temperature increases which suggests fast exchange between enzyme-bound and free P-enolpyruvate. Assuming that the longitudinal electron spin relaxation rate of the gadolinium ion dominates the correlation time for the ternary P-enolpyruvate-gadolinium-enzyme complex, analysis of the relaxation rate data via the Solomon-Bloembergen equations yield a 5.2 A internuclear gadolinium to phosphorus distance.

• OSTI ID: 7276087
• Journal Information: Biochem. Biophys. Res. Commun.; (United States), Journal Name: Biochem. Biophys. Res. Commun.; (United States) Vol. 64:3; ISSN BBRCA
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
BIOCHEMICAL REACTION KINETICS
BIOCHEMISTRY
CARBOXYLIC ACIDS
CHEMISTRY
COMPLEXES
ELEMENTS
ENZYMES
FOURIER TRANSFORMATION
GADOLINIUM
GADOLINIUM COMPLEXES
INTEGRAL TRANSFORMATIONS
KETO ACIDS
KINETICS
MAGNETIC RESONANCE
METALS
MUSCLES
NONMETALS
NUCLEAR MAGNETIC RESONANCE
ORGANIC ACIDS
ORGANIC COMPOUNDS
PHOSPHORUS
PHOSPHOTRANSFERASES
PYRUVIC ACID
RARE EARTH COMPLEXES
RARE EARTHS
REACTION KINETICS
RELAXATION
RESONANCE
SPIN-SPIN RELAXATION
TRANSFERASES
TRANSFORMATIONS