Evidence map›Paper›PMID 23859602›Full record

ArticleJournal of the American Chemical Society2013

Electron flow through nitrotyrosinate in Pseudomonas aeruginosa azurin.

Jeffrey J Warren, Nadia Herrera, Michael G Hill, Jay R Winkler, Harry B Gray

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

24 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Hole Hopping Across a Protein-Protein Interface.The journal of physical chemistry. B · 2019
    Article
  9. Article
  10. Fluctuating hydrogen-bond networks govern anomalous electron transfer kinetics in a blue copper protein.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  11. Article
  12. Article
  13. Article
  14. Redox Signaling through DNA.Israel journal of chemistry · 2016
    Article
  15. Article
  16. Article
  17. Proton-coupled electron hopping in Ru-modified P. aeruginosa azurin.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016
    Article
  18. Review
  19. Could tyrosine and tryptophan serve multiple roles in biological redox processes?Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2015
    Article
  20. Review
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

5 authors at 2 institutions in 1 country.

Jeffrey J WarrenBeckman Institute and Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California 91125, USA.
Nadia Herrera
Michael G Hill
Jay R Winkler
Harry B Gray
California Institute of Technology · USOccidental College · US

Funding

ZWITTERION SURFACTANT DDMAB FOR IMPROV STABIL OF PROTEINP41RR001209 · NCRR · STANFORD UNIVERSITY · PI GONZALEZ, ANA M · 1985 to 2011
$38.9M
ELECTRON-TRANSFER PROCESSES IN IRON AND COPPER PROTEINSR01DK019038 · NIDDK · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI GRAY, HARRY B, WINKLER, JAY R · 1986 to 2023
$7.0M
ELECTRON TRANSFER PROCESSES IN IRON AND COPPER PROTEINSR37DK019038 · NIDDK · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI GRAY, HARRY B · 1996 to 2003
$1.2M
Tyrosine Assisted Electron Transfer in Modified AzurinsF32GM095037 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI WARREN, JEFFREY JOHN · 2010 to 2012
$142k
NCRR NIH HHS P41 RR001209NIDDK NIH HHS DK019038NIDDK NIH HHS R01 DK019038NIDDK NIH HHS R37 DK019038NIGMS NIH HHS F32 GM095037NIGMS NIH HHS GM095037
6 · The paper itself

Abstract

We have designed ruthenium-modified Pseudomonas aeruginosa azurins that incorporate 3-nitrotyrosine (NO2YOH) between Ru(2,2'-bipyridine)2(imidazole)(histidine) and Cu redox centers in electron transfer (ET) pathways. We investigated the structures and reactivities of three different systems: RuH107NO2YOH109, RuH124NO2YOH122, and RuH126NO2YOH122. RuH107NO2YOH109, unlabeled H124NO2YOH122, and unlabeled H126NO2YOH122 were structurally characterized. The pKa's of NO2YOH at positions 122 and 109 are 7.2 and 6.0, respectively. Reduction potentials of 3-nitrotyrosinate (NO2YO(-))-modified azurins were estimated from cyclic and differential pulse voltammetry data: oxidation of NO2YO(-)122 occurs near 1.1 versus NHE; oxidation of NO2YO(-)109 is near 1.2 V. Our analysis of transient optical spectroscopic experiments indicates that hopping via NO2YO(-) enhances Cu(I) oxidation rates over single-step ET by factors of 32 (RuH107NO2YO(-)109), 46 (RuH126NO2YO(-)122), and 13 (RuH124NO2YO(-)122).

Indexed as

Pseudomonas aeruginosaAzurinCopperElectron TransportModels, MolecularOrganometallic CompoundsProtein ConformationTyrosine3-nitrotyrosineAzurinCopperOrganometallic CompoundsTyrosine

Identifiers

PMID23859602
PMCPMC3839300
OpenAlexW1970213384

What OpenQuestion holds

Textmetadata
LicenceTDM
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.