The metal dependence of single-metal mediated phosphodiester bond cleavage: a QM/MM study of a multifaceted human enzyme-Reference-Cited by-同舟云学术

The metal dependence of single-metal mediated phosphodiester bond cleavage: a QM/MM study of a multifaceted human enzyme

Published:2022 Issue:47 Volume:24 Page:29130-29140
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Kaur Rajwinder¹^ORCID,Aboelnga Mohamed M.¹^ORCID,Nikkel Dylan J.¹^ORCID,Wetmore Stacey D.¹^ORCID

Affiliation:

1. Department of Chemistry and Biochemistry, University of Lethbridge, 4401 University Drive West, Lethbridge, Alberta, T1K 3M4, Canada

Abstract

QM/MM calculations rationalize the experimentally-observed metal dependence of a unique endonuclease that uses only a single metal to break the inherently stable phosphodiester bond in nucleic acids.

Funder

Natural Sciences and Engineering Research Council of Canada

University of Lethbridge

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2022/CP/D2CP04338F

Reference96 articles.

1. Phosphodiester models for cleavage of nucleic acids

2. Catalytic Metal Ions and Enzymatic Processing of DNA and RNA

3. Nucleases: diversity of structure, function and mechanism

4. One is enough: insights into the two-metal ion nuclease mechanism from global analysis and computational studies

5. Unraveling the three-metal-ion catalytic mechanism of the DNA repair enzyme endonuclease IV

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