Evidence map›Paper›PMID 18458965›Full record

ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2008

Assignment of the ferriheme resonances of high- and low-spin forms of the symmetrical hemin-reconstituted nitrophorins 1-4 by 1H and 13C NMR spectroscopy: the dynamics of heme ruffling deformations.

Tatiana K Shokhireva, Nikolai V Shokhirev, Robert E Berry, Hongjun Zhang, F Ann Walker

Abstract read
PubMed Publisher
In one paragraph

Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2008. 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
1.2field-weighted citation impact, top 24% 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, 22 citations in OpenAlex.

  1. Influence of heme c attachment on heme conformation and potential.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018
    Article
  2. Article
  3. Article
  4. Article
  5. NMR investigations of nitrophorin 2 belt side chain effects on heme orientation and seating of native N-terminus NP2 and NP2(D1A).Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. 1H and 13C NMR spectroscopic studies of the ferriheme resonances of three low-spin complexes of wild-type nitrophorin 2 and nitrophorin 2(V24E) as a function of pH.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2009
    Article
  17. Article
  18. 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

5 authors at 1 institution in 1 country.

Tatiana K ShokhirevaDepartment of Chemistry, The University of Arizona, Tucson, AZ 85721-0041, USA.
Nikolai V Shokhirev
Robert E Berry
Hongjun Zhang
F Ann Walker
University of Arizona · US

Funding

NITRIC OXIDE INTERACTION WITH INSECT NITROPHORINSR01HL054826 · NHLBI · UNIVERSITY OF ARIZONA · PI WALKER, FRANCES ANN · 1995 to 2012
$3.5M
NHLBI NIH HHS HL054826
6 · The paper itself

Abstract

The four major nitrophorins (NPs) of the adult blood-sucking insect Rhodnius prolixus have been reconstituted with the "symmetrical hemin" 2,4-dimethyldeuterohemin, and their NMR spectra have been investigated as the high-spin (S=5/2) aqua and low-spin (S=1/2) N-methylimidazole (NMeIm) and cyanide complexes. The NMeIm complexes allow assignment of the high-spin hemin resonances by saturation transfer difference spectroscopy. The cyanide complexes were investigated as paramagnetic analogues of the NO complexes. It is shown that the hemin ring is highly distorted from planarity, much more so for NP2 than for NP1 and NP4 (with ruffling being the major distortion mode), for both high- and low-spin forms. For the cyanide complexes, the conformation of the distorted ring changes on the NMR timescale to yield chemical exchange (exchange spectroscopy, EXSY) cross peaks for NP1sym(CN), NP3sym(CN) and NP4sym(CN) but not for NP2sym(CN). These changes in nonplanar conformation are visualized as a "rolling" of the ruffled macrocycle ridges through some number of degrees, the lowest-energy ruffling mode. This probably occurs in response to slow protein dynamics that cause the I120 and L132 side chains in the distal heme pocket to move in opposite directions (up and away vs. down and toward the hemin ring). This in turn changes the out-of-plane displacements of the 2M and 3M of the symmetrical hemin on the NMR timescale. Two other types of dynamics, i.e., changes in heme seating and NMeIm rotation, are also observed. The highly distorted heme and the dynamics it causes are unique to the NPs and a few other heme proteins with highly distorted macrocycles.

Indexed as

Quantum TheoryAnimalsCarbon IsotopesCyanidesHemeHemeproteinsHeminImidazolesMagnetic Resonance SpectroscopyModels, ChemicalProtein ConformationProtonsReference StandardsRhodniusSalivary Proteins and Peptides1-methylimidazoleCarbon IsotopesCyanidesHemeHemeproteinsHeminImidazolesnitrophorinProtonsSalivary Proteins and Peptides

Identifiers

PMID18458965
OpenAlexW2051696314

What OpenQuestion holds

Textmetadata
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.