ArticleJournal of the American Chemical Society2010
Site-specific incorporation of 3-nitrotyrosine as a probe of pKa perturbation of redox-active tyrosines in ribonucleotide reductase.
Article in Journal of the American Chemical Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 89 citations in OpenAlex.
- Efficient and Site-Specific Incorporation of 3-Nitro-Tyrosine Into Recombinant Proteins inBio-protocol · 2026Article
- Genetic Incorporation of Diverse Noncanonical Amino Acids for Histidine Substitution.Journal of the American Chemical Society · 2026Article
- Real-time assay of ribonucleotide reductase activity with a fluorescent RNA aptamer.FEBS letters · 2026Article
- Radical-Mediated Nucleophilic Peptide Cross-Linking in Dynobactin Biosynthesis.Journal of the American Chemical Society · 2024Article
- 2.6-Å resolution cryo-EM structure of a class Ia ribonucleotide reductase trapped with mechanism-based inhibitor NProceedings of the National Academy of Sciences of the United States of America · 2024Article
- 2.6-Å resolution cryo-EM structure of a class Ia ribonucleotide reductase trapped with mechanism-based inhibitor NbioRxiv : the preprint server for biology · 2024Article
- Modulating the pH dependent photophysical properties of green fluorescent protein.RSC advances · 2024Article
- Conformational control over proton-coupled electron transfer in metalloenzymes.Nature reviews. Chemistry · 2024Review
- Mimicking Nonribosomal Peptides from the Marine ActinomyceteACS infectious diseases · 2024Article
- Impact of N221S missense mutation in human ribonucleotide reductase small subunit b on mitochondrial DNA depletion syndrome.Scientific reports · 2023Article
- Radical Transport Facilitated by a Proton Transfer Network at the Subunit Interface of Ribonucleotide Reductase.Journal of the American Chemical Society · 2023Article
- A pilot study on nitration/dysfunction of NK1 segment of myogenic stem cell activator HGF.Biochemistry and biophysics reports · 2022Article
- Exploration ofACS synthetic biology · 2022Article
- In-Cell Characterization of the Stable Tyrosyl Radical in E. coli Ribonucleotide Reductase Using Advanced EPR Spectroscopy.Angewandte Chemie (International ed. in English) · 2021Article
- Detection of Water Molecules on the Radical Transfer Pathway of Ribonucleotide Reductase byJournal of the American Chemical Society · 2021Article
- Computing Proton-Coupled Redox Potentials of Fluorotyrosines in a Protein Environment.The journal of physical chemistry. B · 2021Article
- Conformational Motions and Water Networks at the α/β Interface inJournal of the American Chemical Society · 2020Article
- Subunit Interaction Dynamics of Class Ia Ribonucleotide Reductases: In Search of a Robust Assay.Biochemistry · 2020Article
- Selenocysteine Substitution in a Class I Ribonucleotide Reductase.Biochemistry · 2019Article
- Reductive modification of genetically encoded 3-nitrotyrosine sites in alpha synuclein expressed in E.coli.Redox biology · 2019Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
E. coli ribonucleotide reductase catalyzes the reduction of nucleoside 5'-diphosphates into 2'-deoxynucleotides and is composed of two subunits: alpha2 and beta2. During turnover, a stable tyrosyl radical (Y*) at Y(122)-beta2 reversibly oxidizes C(439) in the active site of alpha2. This radical propagation step is proposed to occur over 35 A, to use specific redox-active tyrosines (Y(122) and Y(356) in beta2, Y(731) and Y(730) in alpha2), and to involve proton-coupled electron transfer (PCET). 3-Nitrotyrosine (NO(2)Y, pK(a) 7.1) has been incorporated in place of Y(122), Y(731), and Y(730) to probe how the protein environment perturbs each pK(a) in the presence of the second subunit, substrate (S), and allosteric effector (E). The activity of each mutant is <4 x 10(-3) that of the wild-type (wt) subunit. The [NO(2)Y(730)]-alpha2 and [NO(2)Y(731)]-alpha2 each exhibit a pK(a) of 7.8-8.0 with E and E/beta2. The pK(a) of [NO(2)Y(730)]-alpha2 is elevated to 8.2-8.3 in the S/E/beta2 complex, whereas no further perturbation is observed for [NO(2)Y(731)]-alpha2. Mutations in pathway residues adjacent to the NO(2)Y that disrupt H-bonding minimally perturb its pK(a). The pK(a) of NO(2)Y(122)-beta2 alone or with alpha2/S/E is >9.6. X-ray crystal structures have been obtained for all [NO(2)Y]-alpha2 mutants (2.1-3.1 A resolution), which show minimal structural perturbation compared to wt-alpha2. Together with the pK(a) of the previously reported NO(2)Y(356)-beta2 (7.5 in the alpha2/S/E complex; Yee, C. et al. Biochemistry 2003, 42, 14541-14552), these studies provide a picture of the protein environment of the ground state at each Y in the PCET pathway, and are the starting point for understanding differences in PCET mechanisms at each residue in the pathway.
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