Supramolecular Stabilization of a Tris(imidazolyl) Zn−Aqua Complex Evidenced by X-ray Analysis: A Structural Model for Mono-Zinc Active Sites of Enzymes-Reference-Cited by-同舟云学术

Supramolecular Stabilization of a Tris(imidazolyl) Zn−Aqua Complex Evidenced by X-ray Analysis: A Structural Model for Mono-Zinc Active Sites of Enzymes

Published:2001-08-01 Issue:34 Volume:123 Page:8442-8443
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Sénèque Olivier¹,Rager Marie-Noëlle¹,Giorgi Michel¹,Reinaud Olivia¹

Affiliation:

1. Laboratoire de Chimie et Biochimie Pharmacologiques et Toxicologiques, CNRS UMR 8601 Université René Descartes, 45 rue des Saints Pères 75270 Paris Cedex 06, France Service de RMN, CNRS UMR 7576 Ecole Nationale Supérieure de Chimie de Paris (ENSCP) 11 rue Pierre et Marie Curie 75231 Paris Cedex 05, France Laboratoire de Cristallochimie, CNRS UMR 6517 Centre Scientifique Saint-Jérôme av. Escadrille Normandie-Niemen 13397 Marseille Cedex 20, France

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja016345e

Reference9 articles.

1. Recent Advances in Zinc Enzymology

2. Protonation of the Hydroxide Ligand in a Synthetic Analogue of Carbonic Anhydrase, [TpBut,Me]ZnOH: Inhibition of Reactivity Towards CO2

3. On the Ligating Properties of Sulfonate and Perchlorate Anions Towards Zinc

4. Calix[6]arenes and Zinc: Biomimetic Receptors for Neutral Molecules

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