Reversible, Long-Range Radical Transfer in E. coli Class Ia Ribonucleotide Reductase
Ribonucleotide reductases (RNRs) catalyze the conversion of nucleotides (NDPs or NTPs where N = C, U, G, or A) to 2′-deoxynucleotides (dNDPs or dNTPs)[superscript 1] and are responsible for controlling the relative ratios and absolute concentrations of cellular dNTP pools. For this reason, RNRs play...
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2017
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Online Access: | http://hdl.handle.net/1721.1/110401 https://orcid.org/0000-0002-4507-1115 https://orcid.org/0000-0001-8076-4489 |
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author | Minnihan, Ellen Catherine Stubbe, JoAnne Nocera, Daniel G. |
author2 | Massachusetts Institute of Technology. Department of Biology |
author_facet | Massachusetts Institute of Technology. Department of Biology Minnihan, Ellen Catherine Stubbe, JoAnne Nocera, Daniel G. |
author_sort | Minnihan, Ellen Catherine |
collection | MIT |
description | Ribonucleotide reductases (RNRs) catalyze the conversion of nucleotides (NDPs or NTPs where N = C, U, G, or A) to 2′-deoxynucleotides (dNDPs or dNTPs)[superscript 1] and are responsible for controlling the relative ratios and absolute concentrations of cellular dNTP pools. For this reason, RNRs play a major role in ensuring the fidelity of DNA replication and repair. RNRs are found in all organisms and are classified based on the metallocofactor used to initiate catalysis,[superscript 1] with the class Ia RNRs requiring a diferric-tyrosyl radical (Y•) cofactor. |
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institution | Massachusetts Institute of Technology |
language | en_US |
last_indexed | 2024-09-23T10:41:05Z |
publishDate | 2017 |
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spelling | mit-1721.1/1104012022-09-30T22:16:56Z Reversible, Long-Range Radical Transfer in E. coli Class Ia Ribonucleotide Reductase Minnihan, Ellen Catherine Stubbe, JoAnne Nocera, Daniel G. Massachusetts Institute of Technology. Department of Biology Massachusetts Institute of Technology. Department of Chemistry Minnihan, Ellen Catherine Nocera, Daniel G Stubbe, JoAnne Ribonucleotide reductases (RNRs) catalyze the conversion of nucleotides (NDPs or NTPs where N = C, U, G, or A) to 2′-deoxynucleotides (dNDPs or dNTPs)[superscript 1] and are responsible for controlling the relative ratios and absolute concentrations of cellular dNTP pools. For this reason, RNRs play a major role in ensuring the fidelity of DNA replication and repair. RNRs are found in all organisms and are classified based on the metallocofactor used to initiate catalysis,[superscript 1] with the class Ia RNRs requiring a diferric-tyrosyl radical (Y•) cofactor. National Institutes of Health (U.S.) (GM47274) National Institutes of Health (U.S.) (GM29595) 2017-06-30T19:17:44Z 2017-06-30T19:17:44Z 2013-06 2013-02 Article http://purl.org/eprint/type/JournalArticle 0001-4842 1520-4898 http://hdl.handle.net/1721.1/110401 Minnihan, Ellen C., Daniel G. Nocera, and JoAnne Stubbe. “Reversible, Long-Range Radical Transfer in E. Coli Class Ia Ribonucleotide Reductase.” Acc. Chem. Res. 46, no. 11 (November 19, 2013): 2524–2535. https://orcid.org/0000-0002-4507-1115 https://orcid.org/0000-0001-8076-4489 en_US http://dx.doi.org/10.1021/ar4000407 Accounts of Chemical Research Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use. application/pdf American Chemical Society (ACS) PMC |
spellingShingle | Minnihan, Ellen Catherine Stubbe, JoAnne Nocera, Daniel G. Reversible, Long-Range Radical Transfer in E. coli Class Ia Ribonucleotide Reductase |
title | Reversible, Long-Range Radical Transfer in E. coli Class Ia Ribonucleotide Reductase |
title_full | Reversible, Long-Range Radical Transfer in E. coli Class Ia Ribonucleotide Reductase |
title_fullStr | Reversible, Long-Range Radical Transfer in E. coli Class Ia Ribonucleotide Reductase |
title_full_unstemmed | Reversible, Long-Range Radical Transfer in E. coli Class Ia Ribonucleotide Reductase |
title_short | Reversible, Long-Range Radical Transfer in E. coli Class Ia Ribonucleotide Reductase |
title_sort | reversible long range radical transfer in e coli class ia ribonucleotide reductase |
url | http://hdl.handle.net/1721.1/110401 https://orcid.org/0000-0002-4507-1115 https://orcid.org/0000-0001-8076-4489 |
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