Evidence map›Paper›PMID 22711806›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Structure/function correlations among coupled binuclear copper proteins through spectroscopic and reactivity studies of NspF.

Jake W Ginsbach, Matthew T Kieber-Emmons, Ryohei Nomoto, Akio Noguchi, Yasuo Ohnishi, Edward I Solomon

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed.

  1. Structural insights intoInorganic chemistry frontiers · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Intramolecular Phenolic H-Atom Abstraction by a NJournal of the American Chemical Society · 2024
    Article
  9. Article
  10. Article
  11. Review
  12. Elucidation of the tyrosinase/OProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  13. Article
  14. Evidence for H-bonding interactions to the μ-ηChemical communications (Cambridge, England) · 2022
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Activation of dioxygen by copper metalloproteins and insights from model complexes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017
    Review
  20. Review
4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

6 authors.

Jake W GinsbachDepartment of Chemistry, Stanford University, Stanford, CA 94305, USA.
Matthew T Kieber-Emmons
Ryohei Nomoto
Akio Noguchi
Yasuo Ohnishi
Edward I Solomon

Funding

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
Spectroscopic and Computational Investigation of Cytrochrome C Oxidase and ModelsF32GM085914 · NIGMS · STANFORD UNIVERSITY · PI KIEBER-EMMONS, MATTHEW THOMAS · 2010 to 2011
$99k
NIDDK NIH HHS DK31450NIDDK NIH HHS R01 DK031450NIDDK NIH HHS R37 DK031450NIGMS NIH HHS F32 GM085914NIGMS NIH HHS GM085914
6 · The paper itself

Abstract

The terminal step of 4-hydroxy-3-nitrosobenzamide biosynthesis in Streptomyces murayamaensis is performed by NspF, a mono-oxygenase that converts o-aminophenols to the corresponding nitroso product (hydroxyanilinase activity). Previous biochemical characterization of the resting form of NspF suggested that this enzyme belonged to the coupled binuclear copper enzyme (CBC) family. Another member of this enzyme family, tyrosinase, is able to mono-oxygenate monophenols (monophenolase activity) but not o-aminophenols. To gain insight into the unique reactivity of NspF, we have generated and characterized the oxy form of its active site. The observation of spectral features identical to those of oxy-tyrosinase indicates that oxy-NspF contains a Cu(2)O(2) core where peroxide is coordinated in a μ-η(2):η(2) mode, confirming that NspF is a CBC enzyme. This oxy form is found to react with monophenols, indicating that, like tyrosinase, NspF also possesses monophenolase activity. A comparison of the two electrophilic mechanisms for the monophenolase and hydroxyanilinase activity indicates a large geometric change between their respective transition states. The potential for specific interactions between the protein pocket and the substrate in each transition state is discussed within the context of the differential reactivity of this family of enzymes with equivalent μ-η(2):η(2) peroxy bridged coupled binuclear copper active sites.

Indexed as

Amine Oxidase (Copper-Containing)AminophenolsBacterial ProteinsBenzamidesCatalytic DomainCopperMonophenol MonooxygenaseNitroso CompoundsOxygenProtein Structure, TertiarySpectrum Analysis, RamanStreptomycesStructure-Activity RelationshipSubstrate Specificity3-nitrosobenzamideAmine Oxidase (Copper-Containing)AminophenolsBacterial ProteinsBenzamidesCopperMonophenol MonooxygenaseNitroso CompoundsOxygen

Identifiers

PMID22711806
PMCPMC3390868

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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.