Project: Research project

Project Details


We propose to study how substrates bind to enzymes during catalysis using
Resonance Raman Spectroscopy. Resonance Raman Spectroscopy can yield
detailed information concerning the molecular properties of in situ
substrates unavailable by other methods. We have recently obtained Raman
spectrum of reduced nicotinamide adenine dinucleotide (NADH) when bound to
liver alcohol dehydrogenase (LADH). NADH is the coenzyme to
pyridine-linked dehydrogenase, a major class of enzymes involved in all
areas of metabolism. Marked changes in the Raman spectrum of NADH occur
when it forms the binary LADH/NADH complex. We intend to obtain and
understand the Raman spectra of NADH and NAD+ (the oxidized form of NADH)
when bound to the active sites of selected dehydrogenases. We also intend
to study the changes in the Raman spectrum of the aldehyde substrates of
LADH upon binding. We have selected two such substrates: retinal, a
relatively good substrate of LADH, and DABA, a relatively poor one. These
studies can greatly enhance our understanding of how enzymes function on a
molecular level.

We also propose to develop a coherent theoretical program to interpret our
data in detailed molecular terms.
Effective start/end date1/1/907/31/00


  • National Institute of General Medical Sciences
  • National Institute of General Medical Sciences


  • Catalysis
  • Spectroscopy


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