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The Conformation of NAD+ Bound to Lactate Dehydrogenase Determined by Nuclear Magnetic Resonance with Suppression of Spin Diffusion

Sebastien J. F. Vincent, Catherine Zwahlen, Carol Beth Post, John W. Burgner and Geoffrey Bodenhausen
Proceedings of the National Academy of Sciences of the United States of America
Vol. 94, No. 9 (Apr. 29, 1997), pp. 4383-4388
Stable URL: http://www.jstor.org/stable/42019
Page Count: 6
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
The Conformation of NAD+ Bound to Lactate Dehydrogenase Determined by Nuclear Magnetic Resonance with Suppression of Spin Diffusion
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Abstract

We have reinvestigated the conformation of NAD+ bound to dogfish lactate dehydrogenase (LDH) by using an NMR experiment that allows one to exploit nuclear Overhauser effects to determine internuclear distances between pairs of protons, without perturbation of spin-diffusion effects from other protons belonging either to the cofactor or to the binding pocket of the enzyme. The analysis indicates that the structure of bound NAD+ is in accord with the conformation determined in the solid state by x-ray diffraction for the adenosine moiety, but deviates significantly from that of the nicotinamide. The NMR data indicate conformational averaging about the glycosidic bond of the nicotinamide nucleotide. In view of the strict stereospecificity of catalysis by LDH and the conformational averaging of bound NAD+ that we infer from solution-state NMR, we suggest that LDH binds the cofactor in both syn and anti conformations, but that binding interactions in the syn conformation are not catalytically productive.

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