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Magnetic resonance studies of enzymesubstrate complexes with paramagnetic probes as illustrated by creatine kinase

Published online by Cambridge University Press:  17 March 2009

Mildred Cohn
Mildred Cohn
Affiliation:
Johnson Research Foundation, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104
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Extract

Only two spectroscopic methods are capable of detecting individual atoms in macromolecular systems, X-ray diffraction in the crystalline state and nuclear magnetic resonance (NMR) in the liquid state. For an enzyme-substrate complex, X-ray diffraction can yield information on the geometric structure at the active site and nuclear magnetic resonance absorption can, in principle, yield information on the electronic structure at the active site and on the conformation of enzyme-substrate complexes. Both types of information are needed for unraveling the mechanism of enzyme catalysis on the molecular level. The exciting successes of X-ray diffraction in delineating active sites are already established; NMR, a comparative latecomer among spectroscopic techniques is just beginning to demonstrate its potentialities. McDonald & Phillips have summarized in their excellent review (1969) the work on direct observation of hydrogen atoms (protons) by NMR spectroscopy which has advanced our knowledge of protein structure. The extensive studies of Jardetzky and his co-workers on the NMR of ribonuclease and its inhibitor complexes has culminated in a suggested mechanism of catalytic action (Roberts et al. 1969).

Type
Research Article
Information
Quarterly Reviews of Biophysics , Volume 3 , Issue 1 , February 1970 , pp. 61 - 89
Copyright
Copyright © Cambridge University Press 1970

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