Evidence map›Paper›PMID 25666062›Full record

ArticlePhilosophical transactions. Series A, Mathematical, physical, and engineering sciences2015

Could tyrosine and tryptophan serve multiple roles in biological redox processes?

Jay R Winkler, Harry B Gray

Abstract read
In one paragraph

Article in Philosophical transactions. Series A, Mathematical, physical, and engineering sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
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

14 citing papers in PubMed.

  1. Empowering Precision C-H Functionalization: Advances in Peroxygenase Engineering.Angewandte Chemie (International ed. in English) · 2026
    Review
  2. Article
  3. Article
  4. Does Tyrosine ProtectThe journal of physical chemistry. B · 2022
    Article
  5. Article
  6. Review
  7. Article
  8. Oxalate decarboxylase uses electron hole hopping for catalysis.The Journal of biological chemistry · 2021
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. The Rise of Radicals in Bioinorganic Chemistry.Israel journal of chemistry · 2016
    Article
  14. Defusing redox bombs?Proceedings of the National Academy of Sciences of the United States of America · 2015
    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

2 authors.

Jay R WinklerBeckman Institute, California Institute of Technology, 1200 East California Boulevard, Pasadena, CA 91125, USA.
Harry B GrayBeckman Institute, California Institute of Technology, 1200 East California Boulevard, Pasadena, CA 91125, USA hbgray@caltech.edu.

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 DK-019038NIDDK NIH HHS R01 DK019038
6 · The paper itself

Abstract

Single-step electron tunnelling reactions can transport charges over distances of 15-20 Åin proteins. Longer-range transfer requires multi-step tunnelling processes along redox chains, often referred to as hopping. Long-range hopping via oxidized radicals of tryptophan and tyrosine, which has been identified in several natural enzymes, has been demonstrated in artificial constructs of the blue copper protein azurin. Tryptophan and tyrosine serve as hopping way stations in high-potential charge transport processes. It may be no coincidence that these two residues occur with greater-than-average frequency in O(2)- and H(2)O(2)-reactive enzymes. We suggest that appropriately placed tyrosine and/or tryptophan residues prevent damage from high-potential reactive intermediates by reduction followed by transfer of the oxidizing equivalent to less harmful sites or out of the protein altogether.

Indexed as

Oxidation-ReductionAzurinCopperElectronsHydrogen PeroxideMolecular ConformationOxygenPseudomonas aeruginosaTryptophanTyrosineAzurinCopperHydrogen PeroxideOxygenTryptophanTyrosineazurincytochrome P450electron transferhoppingprotein radical

Identifiers

PMID25666062
PMCPMC4342971

What OpenQuestion holds

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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.