Volume 56, Issue 6 pp. 726-728

The oxidized form of nicotin­amide adenine dinucleotide

Benoit Guillot

Benoit Guillot

Laboratoire de Cristallographie et Modélisation des Matériaux Minéraux et Biologiques (LCM 3 B), UPRESA No. 7036, Université Henri Poincaré, Nancy 1, Faculté des Sciences, BP 239, 54506 Vandoeuvre lès Nancy CEDEX, France

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Christian Jelsch

Christian Jelsch

Laboratoire de Cristallographie et Modélisation des Matériaux Minéraux et Biologiques (LCM 3 B), UPRESA No. 7036, Université Henri Poincaré, Nancy 1, Faculté des Sciences, BP 239, 54506 Vandoeuvre lès Nancy CEDEX, France

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Claude Lecomte

Claude Lecomte

Laboratoire de Cristallographie et Modélisation des Matériaux Minéraux et Biologiques (LCM 3 B), UPRESA No. 7036, Université Henri Poincaré, Nancy 1, Faculté des Sciences, BP 239, 54506 Vandoeuvre lès Nancy CEDEX, France

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First published: 30 June 2004
Citations: 3
Christian Jelsch, e-mail: [email protected]

Abstract

The crystal structure of the free acid form of NAD+ tetrahydrate (nicotin­amide adenine dinucleotide tetrahydrate or 3-carbamoyl-1-β-d-ribo­furan­osyl­pyridinium hydro­xide 5′-ester with adenosine 5′-pyrophosphate inner salt tetrahydrate, C21H27N7O14P2·4H2O) has been determined at 100 K. NAD+ is the coenzyme of several protein families and plays a dominant role in biological redox processes. In this study, the mol­ecule shows a different conformation from the one usually found in holoenzyme complexes.

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