The Limitations of X-ray Absorption Spectroscopy for Determining the Structure of Zinc Sites in Proteins. When Is a Tetrathiolate Not a Tetrathiolate?-Reference-Cited by-同舟云学术

The Limitations of X-ray Absorption Spectroscopy for Determining the Structure of Zinc Sites in Proteins. When Is a Tetrathiolate Not a Tetrathiolate?

Published:1998-08-01 Issue:33 Volume:120 Page:8401-8409
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Clark-Baldwin Kimber¹,Tierney David L.¹,Govindaswamy Nandakumar¹,Gruff Eric S.¹,Kim Chongwoo¹,Berg Jeremy¹,Koch Stephen A.¹,Penner-Hahn James E.¹

Affiliation:

1. Contribution from the Departments of Chemistry, The University of Michigan, Ann Arbor, Michigan 48109-1055, State University of New York at Stonybrook, Stonybrook, New York 11974-3400, and The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja980580o

Reference59 articles.

1. Zinc coordination, function, and structure of zinc enzymes and other proteins

2. Active-site zinc ligands and activated H2O of zinc enzymes.

3. Zinc(II) coordination domain mutants of T4 gene 32 protein

4. Metal binding ‘finger’ structures in the glucocorticoid receptor defined by site-directed mutagenesis.

5. Site-directed mutagenesis of Escherichia coli tRNA-Guanine Transglycosylase zinc metalloprotein to identify zinc ligands

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