Subunit Interaction Dynamics of Class Ia Ribonucleotide Reductases: In Search of a Robust Assay-Reference-Cited by-同舟云学术

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Subunit Interaction Dynamics of Class Ia Ribonucleotide Reductases: In Search of a Robust Assay

Published:2020-03-18 Issue:14 Volume:59 Page:1442-1453
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Ravichandran Kanchana¹^ORCID,Olshansky Lisa¹²,Nocera Daniel G.²^ORCID,Stubbe JoAnne¹³^ORCID

Affiliation:

1. Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, United States

2. Department of Chemistry and Chemical Biology, Harvard University, 12 Oxford Street, Cambridge, Massachusetts 02138, United States

3. Department of Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, United States

Funder

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.0c00001

Reference67 articles.

1. Protein Radicals in Enzyme Catalysis

2. RIBONUCLEOTIDE REDUCTASES

3. Structure of ribonucleotide reductase protein R1

4. Three-dimensional structure of the free radical protein of ribonucleotide reductase

5. Ribonucleotide Reductases: Structure, Chemistry, and Metabolism Suggest New Therapeutic Targets

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1. Conformational control over proton-coupled electron transfer in metalloenzymes;Nature Reviews Chemistry;2024-09-02

2. Conformational Landscapes of a Class I Ribonucleotide Reductase Complex during Turnover Reveal Intrinsic Dynamics and Asymmetry;2024-06-17

3. Structural insights into the half-of-sites reactivity in homodimeric and homotetrameric metalloenzymes;Current Opinion in Chemical Biology;2023-08

4. Characterization of Stenotrophomonas maltophilia phage AXL1 as a member of the genus Pamexvirus encoding resistance to trimethoprim–sulfamethoxazole;Scientific Reports;2022-06-18

5. Kinetic model for reversible radical transfer in ribonucleotide reductase;Proceedings of the National Academy of Sciences;2022-06-17

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