Evidence map›Paper›PMID 27325093›Full record

ArticleNature chemistry2016

Reversible S-nitrosylation in an engineered azurin.

Shiliang Tian, Jing Liu, Ryan E Cowley, Parisa Hosseinzadeh, Nicholas M Marshall, Yang Yu, Howard Robinson, Mark J Nilges, Ninian J Blackburn, Edward I Solomon and 1 more

Open access · greenAbstract read
In one paragraph

Article in Nature chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Catalysis and Electron Transfer inChemical reviews · 2022
    Review
  8. Article
  9. Article
  10. Article
  11. Catalysis and Electron Transfer in De Novo Designed Helical Scaffolds.Angewandte Chemie (International ed. in English) · 2020
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
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  18. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 4 institutions in 1 country.

Shiliang TianDepartment of Chemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, Illinois 61801, USA.
Jing LiuDepartment of Chemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, Illinois 61801, USA.
Ryan E CowleyDepartment of Chemistry, Stanford University, Stanford, California 94305, USA.
Parisa HosseinzadehDepartment of Biochemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, Illinois 61801, USA.
Nicholas M MarshallDepartment of Chemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, Illinois 61801, USA.
Yang YuCenter of Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, Illinois 61801, USA.ORCID 0000-0002-0784-9715
Howard RobinsonDepartment of Biology, Brookhaven National Laboratory, Upton, New York 11973, USA.
Mark J NilgesDepartment of Chemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, Illinois 61801, USA.
Ninian J BlackburnInstitute of Environmental Health, Oregon Health &Sciences University, Portland, Oregon 97239, USA.
Edward I SolomonDepartment of Chemistry, Stanford University, Stanford, California 94305, USA.
Yi LuDepartment of Chemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, Illinois 61801, USA.
University of Illinois Urbana-Champaign · USStanford University · USBrookhaven National Laboratory · USOregon Health & Science University · US

Funding

X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
Structure/Function Correlations Over Copper EnzymesR01DK031450 · NIDDK · STANFORD UNIVERSITY · PI EDWARD I SOLOMON · 1986 to 2026
$8.7M
SPECTROSCOPIC STUDIES OF COPPER CLUSTERS IN PROTEINSR37DK031450 · NIDDK · STANFORD UNIVERSITY · PI SOLOMON, EDWARD I · 1994 to 2011
$5.7M
X-RAY SPECTROSCOPIC STUDIES ON HEME-COPPER OXIDASESR01GM054803 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI BLACKBURN, NINIAN J · 1997 to 2015
$3.2M
NIDDK NIH HHS R01 DK031450NIDDK NIH HHS R37 DK031450NIGMS NIH HHS P41 GM103393NIGMS NIH HHS R01 GM054803
6 · The paper itself

Abstract

S-Nitrosothiols are known as reagents for NO storage and transportation and as regulators in many physiological processes. Although the S-nitrosylation catalysed by haem proteins is well known, no direct evidence of S-nitrosylation in copper proteins has been reported. Here, we report reversible insertion of NO into a copper-thiolate bond in an engineered copper centre in Pseudomonas aeruginosa azurin by rational design of the primary coordination sphere and tuning its reduction potential by deleting a hydrogen bond in the secondary coordination sphere. The results not only provide the first direct evidence of S-nitrosylation of Cu(II)-bound cysteine in metalloproteins, but also shed light on the reaction mechanism and structural features responsible for stabilizing the elusive Cu(I)-S(Cys)NO species. The fast, efficient and reversible S-nitrosylation reaction is used to demonstrate its ability to prevent NO inhibition of cytochrome bo3 oxidase activity by competing for NO binding with the native enzyme under physiologically relevant conditions.

Indexed as

AzurinCopperCysteineHydrogen BondingMetalloproteinsNitric OxidePseudomonas aeruginosaS-NitrosothiolsAzurinCopperCysteineMetalloproteinsNitric OxideS-Nitrosothiols

Identifiers

PMID27325093
PMCPMC4918514
OpenAlexW2344156231

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.