Share Email Print
cover

Proceedings Paper

Dehydrogenase enzyme/coenzyme/substrate interactions
Author(s): Ronald E. Hester; J. C. Austin
Format Member Price Non-Member Price
PDF $14.40 $18.00
cover GOOD NEWS! Your organization subscribes to the SPIE Digital Library. You may be able to download this paper for free. Check Access

Paper Abstract

Resonance Raman spectra of several apo and holodehydrogenase enzymes excited with ultraviolet laser wavelengths are reported. At 260 nm maximum selective enhancement of the NAD and NADH coenzyme vibrational spectra is seen and effects associated with the coenzyme binding to the several different enzymes are attributed to polarity and hydrogen bonding between adenine component and amino acid residues at the enzyme binding sites. With 220 nm excitation the aromatic amino acid residues dominate the RR vibrational spectra while 240 nm excitation is selected to probe the acyl enzyme intermediate in the reaction of glyceraldehyde3phosphate dehydrogenase (GAPDH) with its substrate GAP. Comparisons are made with recent results from normal nonresonance Raman studies and finally new data on inelastic neutron scattering (INS) are presented. 2.

Paper Details

Date Published: 1 May 1991
PDF: 7 pages
Proc. SPIE 1403, Laser Applications in Life Sciences, (1 May 1991); doi: 10.1117/12.57364
Show Author Affiliations
Ronald E. Hester, Univ. of York (United Kingdom)
J. C. Austin, Princeton Univ. (United States)


Published in SPIE Proceedings Vol. 1403:
Laser Applications in Life Sciences
Sergei A. Akhmanov; Marina Yu. Poroshina, Editor(s)

© SPIE. Terms of Use
Back to Top