Zinc Solid-State NMR Spectroscopy of Human Carbonic Anhydrase: Implications for the Enzymatic Mechanism-Reference-Cited by-同舟云学术

Zinc Solid-State NMR Spectroscopy of Human Carbonic Anhydrase: Implications for the Enzymatic Mechanism

Published:2004-03-20 Issue:14 Volume:126 Page:4735-4739
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Lipton Andrew S.¹,Heck Robert W.¹,Ellis Paul D.¹

Affiliation:

1. Contribution from the Macromolecular Structure & Dynamics Directorate, W. R. Wiley Environmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, Richland, Washington 99352

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja0305609

Reference36 articles.

1. Zinc: biological functions and coordination motifs

2. Lippard, S. J.; Berg, J. M.Principles of Bioinorganic Chemistry; University Science Books: Mill Valley, California, 1994; Chapter 10, p 269.

3. Carbonic Anhydrase: Evolution of the Zinc Binding Site by Nature and by Design

4. Structure of native and apo carbonic anhydrase II and structure of some of its anion-ligand complexes

5. Carboxylate-histidine-zinc interactions in protein structure and function

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