Evidence map›Paper›PMID 21803041›Full record

ArticleFEBS letters2011

Effect of solution viscosity on intraprotein electron transfer between the FMN and heme domains in inducible nitric oxide synthase.

Wenbing Li, Weihong Fan, Bradley O Elmore, Changjian Feng

Open access · bronzeAbstract read
In one paragraph

Article in FEBS letters, 2011. 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
2.3field-weighted citation impact, top 15% 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

21 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. An isoform-specific pivot modulates the electron transfer between the flavin mononucleotide and heme centers in inducible nitric oxide synthase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020
    Article
  4. Article
  5. Exploring the conformations of nitric oxide synthase with fluorescence.Frontiers in bioscience (Landmark edition) · 2018
    Review
  6. Review
  7. Review
  8. Article
  9. Elucidating nitric oxide synthase domain interactions by molecular dynamics.Protein science : a publication of the Protein Society · 2016
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Nitric oxide synthase domain interfaces regulate electron transfer and calmodulin activation.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  16. Article
  17. Role of an isoform-specific serine residue in FMN-heme electron transfer in inducible nitric oxide synthase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2012
    Article
  18. Article
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Wenbing LiDepartment of Pharmaceutical Sciences, University of New Mexico, Albuquerque, NM 87131, USA.
Weihong Fan
Bradley O Elmore
Changjian Feng
University of New Mexico · US

Funding

NM-INBRE Sequencing and Bioinformatics CoreP20GM103451 · NIGMS · NEW MEXICO STATE UNIVERSITY LAS CRUCES · PI Charlotte C. Gard · 2012 to 2026
$61.2M
ZUNI HEALTH INITIATIVE-PILOT STUDYP20RR016480 · NCRR · NEW MEXICO STATE UNIVERSITY LAS CRUCES · PI GRIFFITH, JEFFREY K · 2001 to 2011
$33.7M
Mechanisms of Electron Transfer in Nitric Oxide Synthases: the Output State in NiR15GM081811 · NIGMS · UNIVERSITY OF NEW MEXICO HEALTH SCIS CTR · PI FENG, CHANGJIAN · 2007 to 2016
$1.0M
Regulation of Nitric Oxide Synthase through Formation of the Output StateR21HL091280 · NHLBI · UNIVERSITY OF NEW MEXICO · PI FENG, CHANGJIAN · 2008 to 2009
$400k
NCRR NIH HHS P20 RR016480NCRR NIH HHS P20RR016480NHLBI NIH HHS HL091280NHLBI NIH HHS R21 HL091280NIGMS NIH HHS GM081811NIGMS NIH HHS P20 GM103451NIGMS NIH HHS R15 GM081811
6 · The paper itself

Abstract

The FMN-heme intraprotein electron transfer (IET) kinetics in a human inducible NOS (iNOS) oxygenase/FMN construct were determined by laser flash photolysis as a function of solution viscosity (1.0-3.0 cP). In the presence of ethylene glycol or sucrose, an appreciable decrease in the IET rate constant value was observed with an increase in the solution viscosity. The IET rate constant is inversely proportional to the viscosity for both viscosogens. This demonstrates that viscosity, and not other properties of the added viscosogens, causes the dependence of IET rates on the solvent concentration. The IET kinetics results indicate that the FMN-heme IET in iNOS is gated by a large conformational change of the FMN domain. The kinetics and NOS flavin fluorescence results together indicate that the docked FMN/heme state is populated transiently.

Indexed as

BuffersElectron TransportEthylene GlycolFlavin MononucleotideHemeHumansKineticsNitric Oxide Synthase Type IIProtein ConformationProtein Structure, TertiarySolutionsSpectrometry, FluorescenceSucroseViscosityBuffersEthylene GlycolFlavin MononucleotideHemeNitric Oxide Synthase Type IISolutionsSucrose

Identifiers

PMID21803041
PMCPMC3163105
OpenAlexW2006980896

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.