Evidence map›Paper›PMID 21469225›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2011

Phototriggering electron flow through Re(I)-modified Pseudomonas aeruginosa azurins.

Ana María Blanco-Rodríguez, Angel J Di Bilio, Crystal Shih, Anna Katrine Museth, Ian P Clark, Michael Towrie, Andrea Cannizzo, Jawahar Sudhamsu, Brian R Crane, Jan Sýkora and 4 more

Open access · greenAbstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

17 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Tryptophan to Tryptophan Hole Hopping in an Azurin Construct.The journal of physical chemistry. B · 2024
    Article
  3. Photoinduced hole hopping through tryptophans in proteins.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  4. Article
  5. Hole Hopping Across a Protein-Protein Interface.The journal of physical chemistry. B · 2019
    Article
  6. Article
  7. Review
  8. Article
  9. Tryptophan-to-heme electron transfer in ferrous myoglobins.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  10. Could tyrosine and tryptophan serve multiple roles in biological redox processes?Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2015
    Article
  11. Article
  12. Review
  13. Tryptophan-accelerated electron flow across a protein-protein interface.Journal of the American Chemical Society · 2013
    Article
  14. Hopping Maps for Photosynthetic Reaction Centers().Coordination chemistry reviews · 2013
    Article
  15. Electron hopping through proteins.Coordination chemistry reviews · 2012
    Article
  16. Article
  17. 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

14 authors at 6 institutions in 4 countries.

Ana María Blanco-RodríguezQueen Mary University of London, School of Biological and Chemical Sciences, Mile End Road, London E1 4NS, UK.
Angel J Di Bilio
Crystal Shih
Anna Katrine Museth
Ian P Clark
Michael Towrie
Andrea Cannizzo
Jawahar Sudhamsu
Brian R Crane
Jan Sýkora
Jay R Winkler
Harry B Gray
Stanislav Záliš
Antonín Vlček
California Institute of Technology · USCornell University · USRutherford Appleton Laboratory · GBCzech Academy of Sciences, J. Heyrovský Institute of Physical Chemistry · CZÉcole Polytechnique Fédérale de Lausanne · CHQueen Mary University of London · GB

Funding

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
NIDDK NIH HHS DK019038NIDDK NIH HHS R01 DK019038NIDDK NIH HHS R37 DK019038
6 · The paper itself

Abstract

The [Re(I)(CO)(3)(4,7-dimethyl-1,10-phenanthroline)(histidine-124)(tryptophan-122)] complex, denoted [Re(I)(dmp)(W122)], of Pseudomonas aeruginosa azurin behaves as a single photoactive unit that triggers very fast electron transfer (ET) from a distant (2 nm) Cu(I) center in the protein. Analysis of time-resolved (ps-μs) IR spectroscopic and kinetics data collected on [Re(I)(dmp)(W122)AzM] (in which M=Zn(II), Cu(II), Cu(I); Az=azurin) and position-122 tyrosine (Y), phenylalanine (F), and lysine (K) mutants, together with excited-state DFT/time-dependent (TD)DFT calculations and X-ray structural characterization, reveal the character, energetics, and dynamics of the relevant electronic states of the [Re(I)(dmp)(W122)] unit and a cascade of photoinduced ET and relaxation steps in the corresponding Re-azurins. Optical population of [Re(I)(imidazole-H124)(CO)(3)]→dmp (1)CT states (CT=charge transfer) is followed by around 110 fs intersystem crossing and about 600 ps structural relaxation to a (3)CT state. The IR spectrum indicates a mixed Re(I)(CO)(3),A→dmp/π→π(*)(dmp) character for aromatic amino acids A122 (A=W, Y, F) and Re(I)(CO)(3)→dmp metal-ligand charge transfer (MLCT) for [Re(I)(dmp)(K122)AzCu(II)]. In a few ns, the (3)CT state of [Re(I)(dmp)(W122)AzM] establishes an equilibrium with the [Re(I)(dmp(.-))(W122(.+))AzM] charge-separated state, (3)CS, whereas the (3)CT state of the other Y, F, and K122 proteins decays to the ground state. In addition to this main pathway, (3)CS is populated by fs- and ps-W(indole)→Re(II) ET from (1)CT and the initially "hot" (3)CT states, respectively. The (3)CS state undergoes a tens-of-ns dmp(.-)→W122(.+) ET recombination leading to the ground state or, in the case of the Cu(I) azurin, a competitively fast (≈30 ns over 1.12 nm) Cu(I)→W(.+) ET, to give [Re(I)(dmp(.-))(W122)AzCu(II)]. The overall photoinduced Cu(I)→Re(dmp) ET through [Re(I)(dmp)(W122)AzCu(I)] occurs over a 2 nm distance in <50 ns after excitation, with the intervening fast (3)CT-(3)CS equilibrium being the principal accelerating factor. No reaction was observed for the three Y, F, and K122 analogues. Although the presence of [Re(dmp)(W122)AzCu(II)] oligomers in solution was documented by mass spectrometry and phosphorescence anisotropy, the kinetics data do not indicate any significant interference from the intermolecular ET steps. The ground-state dmp-indole π-π interaction together with well-matched W/W(.+) and excited-state [Re(II)(CO)(3)(dmp(.-))]/[Re(I)(CO)(3)(dmp(.-))] potentials that result in very rapid electron interchange and (3)CT-(3)CS energetic proximity, are the main factors responsible for the unique ET behavior of [Re(I)(dmp)(W122)]-containing azurins.

Indexed as

ElectronsAzurinCrystallography, X-RayModels, ChemicalMolecular ConformationPhotochemical ProcessesPseudomonas aeruginosaRheniumSpectrophotometry, InfraredAzurinRhenium

Identifiers

PMID21469225
PMCPMC3108028
OpenAlexW2065330526

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Registered trials

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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.