Examination of the relationship of substrate dynamics to enzymic structure, binding energy, and catalysis: NMR studies of adenosine 5 prime -triphosphate and adenylate kinase

Thesis/Dissertation · Thu Dec 31 23:00:00 EST 1987

OSTI ID:7266847

Sanders, II, C R

By measuring the deuterium NMR-relaxation rates of adenylyl ({beta}, {lambda}-methylene)diphosphonic acid (AMPPCP) labeled with deuterium at the adenine ring (8-{sup 2}H)AMPPCP and upon the phosphonate chain (AMPPCD{sub 2}P) free in solution and bound to the MgATP site of adenylate kinases (AK) the local motional dynamics of AMPPCP and MgAMPPCP in the two environments were established. The analysis of the experimental data involved the rigorous experimental verification that the systems studied were in the fast exchange limit on an NMR timescale. In addition analysis required careful examination of the equations describing quadrupolar relaxation, particularly the spectral density equations which contain information on molecular motion. Having determined the local dynamics of the nucleotides and their complexes with Mg + 2 free in solution and bound to AK and observing that MgAMPPCP is an excellent model for the natural substrate of AK, MgATP, we examined the relationship of local substrate dynamics to enzyme structure, binding energy, and catalysis.

• Research Organization: Ohio State Univ., Columbus, OH (USA)
• OSTI ID: 7266847
• Country of Publication: United States
• Language: English

Related Subjects

550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
ATP
CATALYSIS
CHEMICAL BONDS
DEUTERIUM
ENZYMES
HYDROGEN ISOTOPES
ISOTOPE APPLICATIONS
ISOTOPES
LIGHT NUCLEI
MOLECULAR STRUCTURE
NUCLEI
NUCLEOTIDES
ODD-ODD NUCLEI
ORGANIC COMPOUNDS
PHOSPHORUS-GROUP TRANSFERASES
PHOSPHOTRANSFERASES
STABLE ISOTOPES
SUBSTRATES
TRACER TECHNIQUES
TRANSFERASES