ArticleProceedings of the National Academy of Sciences of the United States of America2012
Photo-ribonucleotide reductase β2 by selective cysteine labeling with a radical phototrigger.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 52 citations in OpenAlex.
- Conformational control over proton-coupled electron transfer in metalloenzymes.Nature reviews. Chemistry · 2024Review
- Protein engineering a PhotoRNR chimera based on a unifying evolutionary apparatus among the natural classes of ribonucleotide reductases.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Study and design of amino acid-based radical enzymes using unnatural amino acids.RSC chemical biology · 2023Article
- Radical Transport Facilitated by a Proton Transfer Network at the Subunit Interface of Ribonucleotide Reductase.Journal of the American Chemical Society · 2023Article
- Kinetic model for reversible radical transfer in ribonucleotide reductase.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Radicals in Biology: Your Life Is in Their Hands.Journal of the American Chemical Society · 2021Article
- Gated Proton Release during Radical Transfer at the Subunit Interface of Ribonucleotide Reductase.Journal of the American Chemical Society · 2021Article
- Ribonucleotide Reductases: Structure, Chemistry, and Metabolism Suggest New Therapeutic Targets.Annual review of biochemistry · 2020Review
- Catalysis and Electron Transfer in De Novo Designed Helical Scaffolds.Angewandte Chemie (International ed. in English) · 2020Review
- Selenocysteine Substitution in a Class I Ribonucleotide Reductase.Biochemistry · 2019Article
- A photochemical and theoretical study of the triplet reactivity of furano- and pyrano-1,4-naphthoquionones towards tyrosine and tryptophan derivatives.RSC advances · 2019Article
- Photochemical Rescue of a Conformationally Inactivated Ribonucleotide Reductase.Journal of the American Chemical Society · 2018Article
- High-Frequency/High-Field Electron Paramagnetic Resonance and Theoretical Studies of Tryptophan-Based Radicals.The journal of physical chemistry. A · 2018Article
- Conformationally Dynamic Radical Transfer within Ribonucleotide Reductase.Journal of the American Chemical Society · 2017Article
- Intramolecular Photogeneration of a Tyrosine Radical in a Designed Protein.ChemPhotoChem · 2017Article
- Glutamate 350 Plays an Essential Role in Conformational Gating of Long-Range Radical Transport in Escherichia coli Class Ia Ribonucleotide Reductase.Biochemistry · 2017Article
- Photochemical Generation of a Tryptophan Radical within the Subunit Interface of Ribonucleotide Reductase.Biochemistry · 2016Article
- Charge-Transfer Dynamics at the α/β Subunit Interface of a Photochemical Ribonucleotide Reductase.Journal of the American Chemical Society · 2016Article
- Micelle-Encapsulated Quantum Dot-Porphyrin Assemblies as in Vivo Two-Photon Oxygen Sensors.Journal of the American Chemical Society · 2015Article
- Direct Interfacial YChemical science · 2015Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Photochemical radical initiation is a powerful tool for studying radical initiation and transport in biology. Ribonucleotide reductases (RNRs), which catalyze the conversion of nucleotides to deoxynucleotides in all organisms, are an exemplar of radical mediated transformations in biology. Class Ia RNRs are composed of two subunits: α2 and β2. As a method to initiate radical formation photochemically within β2, a single surface-exposed cysteine of the β2 subunit of Escherichia coli Class Ia RNR has been labeled (98%) with a photooxidant ([Re ] = tricarbonyl(1,10-phenanthroline)(methylpyridyl)rhenium(I)). The labeling was achieved by incubation of S355C-β2 with the 4-(bromomethyl)pyridyl derivative of [Re] to yield the labeled species, [Re]-S355C-β2. Steady-state and time-resolved emission experiments reveal that the metal-to-ligand charge transfer (MLCT) excited-state (3)[Re ](∗) is not significantly perturbed after bioconjugation and is available as a phototrigger of tyrosine radical at position 356 in the β2 subunit; transient absorption spectroscopy reveals that the radical lives for microseconds. The work described herein provides a platform for photochemical radical initiation and study of proton-coupled electron transfer (PCET) in the β2 subunit of RNR, from which radical initiation and transport for this enzyme originates.
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