Evidence map›Paper›PMID 18597456›Full record

ArticleJournal of the American Chemical Society2008

Low-frequency mode activity of heme: femtosecond coherence spectroscopy of iron porphine halides and nitrophorin.

Minoru Kubo, Flaviu Gruia, Abdelkrim Benabbas, Alexander Barabanschikov, William R Montfort, Estelle M Maes, Paul M Champion

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

20 citing papers in PubMed.

  1. Article
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  8. Investigations of heme distortion, low-frequency vibrational excitations, and electron transfer in cytochrome c.Proceedings of the National Academy of Sciences of the United States of America · 2014
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  19. Ultrafast dynamics of diatomic ligand binding to nitrophorin 4.Journal of the American Chemical Society · 2010
    Article
  20. 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
4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

7 authors.

Minoru KuboDepartment of Physics and Center for Interdisciplinary Research on Complex Systems, Northeastern University, Boston, Massachusetts 02115, USA.
Flaviu Gruia
Abdelkrim Benabbas
Alexander Barabanschikov
William R Montfort
Estelle M Maes
Paul M Champion

Funding

NEAR-ULTRAVIOLET RAMAN STUDIES OF CYTOCHROME P450R01DK035090 · NIDDK · NORTHEASTERN UNIVERSITY · PI CHAMPION, PAUL M. · 1986 to 2012
$4.1M
SALIVARY PROTEINS FROM BLOOD-SUCKING INSECTSR01HL062969 · NHLBI · UNIVERSITY OF ARIZONA · PI MONTFORT, WILLIAM R. · 2000 to 2012
$3.4M
NHLBI NIH HHS HL62969NHLBI NIH HHS R01 HL062969NIDDK NIH HHS DK35090NIDDK NIH HHS R01 DK035090
6 · The paper itself

Abstract

The low-frequency mode activity of metalloporphyrins has been studied for iron porphine-halides (Fe(P)(X), X = Cl, Br) and nitrophorin 4 (NP4) using femtosecond coherence spectroscopy (FCS) in combination with polarized resonance Raman spectroscopy and density functional theory (DFT). It is confirmed that the mode symmetry selection rules for FCS are the same as for Raman scattering and that both Franck-Condon and Jahn-Teller mode activities are observed for Fe(P)(X) under Soret resonance conditions. The DFT-calculated low-frequency (20-400 cm (-1)) modes, and their frequency shifts upon halide substitution, are in good agreement with experimental Raman and coherence data, so that mode assignments can be made. The doming mode is located at approximately 80 cm (-1) for Fe(P)(Cl) and at approximately 60 cm (-1) for Fe(P)(Br). NP4 is also studied with coherence techniques, and the NO-bound species of ferric and ferrous NP4 display a mode at approximately 30-40 cm (-1) that is associated with transient heme doming motion following NO photolysis. The coherence spectra of three ferric derivatives of NP4 with different degrees of heme ruffling distortion are also investigated. We find a mode at approximately 60 cm (-1) whose relative intensity in the coherence spectra depends quadratically on the magnitude of the ruffling distortion. To quantitatively account for this correlation, a new "distortion-induced" Raman enhancement mechanism is presented. This mechanism is unique to low-frequency "soft modes" of the molecular framework that can be distorted by environmental forces. These results demonstrate the potential of FCS as a sensitive probe of dynamic and functionally important nonplanar heme vibrational excitations that are induced by the protein environmental forces or by the chemical reactions in the aqueous phase.

Indexed as

BromidesChloridesFerric CompoundsHemeHemeproteinsMetalloporphyrinsModels, MolecularSalivary Proteins and PeptidesSpectrum Analysis, RamanBromidesChloridesFerric CompoundsHemeHemeproteinsMetalloporphyrinsnitrophorinSalivary Proteins and Peptides

Identifiers

PMID18597456
PMCPMC2765994

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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.