Methanethiol Binding Strengths and Deprotonation Energies in Zn(II)–Imidazole Complexes from M05-2X and MP2 Theories: Coordination Number and Geometry Influences Relevant to Zinc Enzymes-Reference-Cited by-同舟云学术

Methanethiol Binding Strengths and Deprotonation Energies in Zn(II)–Imidazole Complexes from M05-2X and MP2 Theories: Coordination Number and Geometry Influences Relevant to Zinc Enzymes

Published:2015-09-04 Issue:37 Volume:119 Page:12182-12192
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Linder Douglas P.¹,Rodgers Kenton R.²

Affiliation:

1. Department of Chemistry and Physics, Southwestern Oklahoma State University, Weatherford, Oklahoma 73096, United States

2. Department of Chemistry and Biochemistry, North Dakota State University, Fargo, North Dakota 58108, United States

Funder

American Heart Association

U.S. Department of Health and Human Services

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.5b07115

Reference56 articles.

1. ZINC PROTEINS: Enzymes, Storage Proteins, Transcription Factors, and Replication Proteins

2. Counting the Zinc-Proteins Encoded in the Human Genome

3. The Zinc proteome: a tale of stability and functionality

4. The ins and outs of biological zinc sites

5. Designing Hydrolytic Zinc Metalloenzymes

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