Evidence map›Paper›PMID 24481708›Full record

ArticleAngewandte Chemie (International ed. in English)2014

Spectroscopic and computational study of a nonheme iron nitrosyl center in a biosynthetic model of nitric oxide reductase.

Saumen Chakraborty, Julian Reed, Matthew Ross, Mark J Nilges, Igor D Petrik, Soumya Ghosh, Sharon Hammes-Schiffer, J Timothy Sage, Yong Zhang, Charles E Schulz and 1 more

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. Article
  2. Article
  3. One-Electron NO to NChemistry (Weinheim an der Bergstrasse, Germany) · 2024
    Article
  4. Engineering an Oxygen-Binding Protein for Photocatalytic COAngewandte Chemie (International ed. in English) · 2023
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Heme redox potentials hold the key to reactivity differences between nitric oxide reductase and heme-copper oxidase.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Design of Heteronuclear Metalloenzymes.Methods in enzymology · 2016
    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

11 authors.

Saumen ChakrabortyDepartment of Chemistry and Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL (USA).
Julian Reed
Matthew Ross
Mark J Nilges
Igor D Petrik
Soumya Ghosh
Sharon Hammes-Schiffer
J Timothy Sage
Yong Zhang
Charles E Schulz
Yi Lu

Funding

Training Program in Chemistry-Interface with BiologyT32GM070421 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI HERGENROTHER, PAUL · 2005 to 2019
$5.4M
DESIGNING HETERONUCLEAR METALLOENZYMESR01GM062211 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI LU, YI · 2001 to 2021
$5.1M
Simulation of Proton and Hydride Transfer in EnzymesR37GM056207 · NIGMS · YALE UNIVERSITY · PI HAMMES-SCHIFFER, SHARON · 2011 to 2020
$3.2M
SIMULATION OF PROTON AND HYDRIDE TRANSFER IN ENZYMESR01GM056207 · NIGMS · UNIVERSITY OF NOTRE DAME · PI HAMMES-SCHIFFER, SHARON · 1998 to 2010
$2.7M
Structure, Spectra, and Roles of Metal and Active Site in HNO Heme Protein CompleR15GM085774 · NIGMS · UNIVERSITY OF SOUTHERN MISSISSIPPI · PI ZHANG, YONG · 2008 to 2021
$1.4M
NIGMS NIH HHS 5T32-GM070421NIGMS NIH HHS GM056207NIGMS NIH HHS GM062211NIGMS NIH HHS GM085774NIGMS NIH HHS R01 GM056207NIGMS NIH HHS R01 GM062211NIGMS NIH HHS R15 GM085774NIGMS NIH HHS R37 GM056207NIGMS NIH HHS T32 GM070421
6 · The paper itself

Abstract

A major barrier to understanding the mechanism of nitric oxide reductases (NORs) is the lack of a selective probe of NO binding to the nonheme FeB center. By replacing the heme in a biosynthetic model of NORs, which structurally and functionally mimics NORs, with isostructural ZnPP, the electronic structure and functional properties of the FeB nitrosyl complex was probed. This approach allowed observation of the first S=3/2 nonheme {FeNO}(7) complex in a protein-based model system of NOR. Detailed spectroscopic and computational studies show that the electronic state of the {FeNO}(7) complex is best described as a high spin ferrous iron (S=2) antiferromagnetically coupled to an NO radical (S=1/2) [Fe(2+)-NO(.)]. The radical nature of the FeB -bound NO would facilitate N-N bond formation by radical coupling with the heme-bound NO. This finding, therefore, supports the proposed trans mechanism of NO reduction by NORs.

Indexed as

AnimalsBinding SitesElectron Spin Resonance SpectroscopyFish ProteinsIronModels, MolecularNitric OxideNitrogen OxidesOxidoreductasesSperm Whaledinitrosyl iron complexFish ProteinsIronNitric Oxidenitric-oxide reductaseNitrogen OxidesOxidoreductasescomputational chemistryEPR spectroscopyheme proteinsironreaction mechanisms

Identifiers

PMID24481708
PMCPMC4048663

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.