Evidence map›Paper›PMID 26627888›Full record

ArticleNature communications2015

A tyrosine-tryptophan dyad and radical-based charge transfer in a ribonucleotide reductase-inspired maquette.

Cynthia V Pagba, Tyler G McCaslin, Gianluigi Veglia, Fernando Porcelli, Jiby Yohannan, Zhanjun Guo, Miranda McDaniel, Bridgette A Barry

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.7field-weighted citation impact, top 15% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

6 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Tyrosine-Rich Peptides as a Platform for Assembly and Material Synthesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2019
    Review
  6. Calcium, conformational selection, and redox-active tyrosine YZ in the photosynthetic oxygen-evolving cluster.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 2 countries.

Cynthia V PagbaSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, Georgia 30332, USA.
Tyler G McCaslinSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, Georgia 30332, USA.
Gianluigi VegliaDepartment of Biochemistry, Biophysics and Molecular Biology, University of Minnesota, Minneapolis, Minnesota 55455, USA.
Fernando PorcelliDepartment of Biochemistry, Biophysics and Molecular Biology, University of Minnesota, Minneapolis, Minnesota 55455, USA.
Jiby YohannanSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, Georgia 30332, USA.
Zhanjun GuoSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, Georgia 30332, USA.
Miranda McDanielSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, Georgia 30332, USA.
Bridgette A BarrySchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, Georgia 30332, USA.
Georgia Institute of Technology · USUniversità degli Studi della Tuscia · ITUniversity of Minnesota · US

Funding

Mapping Allosteric Cooperativity in Protein KinasesR01GM100310 · NIGMS · UNIVERSITY OF MINNESOTA · PI VEGLIA, GIANLUIGI · 2012 to 2019
$4.3M
NIGMS NIH HHS GM-100310NIGMS NIH HHS R01 GM100310
6 · The paper itself

Abstract

In class 1a ribonucleotide reductase (RNR), a substrate-based radical is generated in the α2 subunit by long-distance electron transfer involving an essential tyrosyl radical (Y122O·) in the β2 subunit. The conserved W48 β2 is ∼10 Å from Y122OH; mutations at W48 inactivate RNR. Here, we design a beta hairpin peptide, which contains such an interacting tyrosine-tryptophan dyad. The NMR structure of the peptide establishes that there is no direct hydrogen bond between the phenol and the indole rings. However, electronic coupling between the tyrosine and tryptophan occurs in the peptide. In addition, downshifted ultraviolet resonance Raman (UVRR) frequencies are observed for the radical state, reproducing spectral downshifts observed for β2. The frequency downshifts of the ring and CO bands are consistent with charge transfer from YO· to W or another residue. Such a charge transfer mechanism implies a role for the β2 Y-W dyad in electron transfer.

Indexed as

Amino Acid MotifsElectron TransportEscherichia coliEscherichia coli ProteinsExoribonucleasesHydrogen BondingModels, MolecularTryptophanTyrosineEscherichia coli ProteinsExoribonucleasesrnr protein, E coliTryptophanTyrosine

Identifiers

PMID26627888
PMCPMC4686667
OpenAlexW2340918849

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.