Evidence map›Paper›PMID 29751215›Full record

ArticleJournal of inorganic biochemistry2018

A docked state conformational dynamics model to explain the ionic strength dependence of FMN - heme electron transfer in nitric oxide synthase.

Andrei V Astashkin, Jinghui Li, Huayu Zheng, Yubin Miao, Changjian Feng

Abstract read
In one paragraph

Article in Journal of inorganic biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Analyzing the FMN-heme interdomain docking interactions in neuronal and inducible NOS isoforms by pulsed EPR experiments and conformational distribution modeling.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024
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  6. Generation and characterization of functional phosphoserine-incorporated neuronal nitric oxide synthase holoenzyme.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019
    Article
  7. 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.

Andrei V AstashkinDepartment of Chemistry and Biochemistry, University of Arizona, Tucson, AZ 85721, USA.
Jinghui LiCollege of Pharmacy, University of New Mexico, Albuquerque, NM 87131, USA.
Huayu ZhengCollege of Pharmacy, University of New Mexico, Albuquerque, NM 87131, USA; Department of Chemistry and Chemical Biology, University of New Mexico, Albuquerque, NM 87131, USA.
Yubin MiaoDepartment of Radiology, School of Medicine, University of Colorado Denver, Aurora, CO 80045, USA.
Changjian FengCollege of Pharmacy, University of New Mexico, Albuquerque, NM 87131, USA; Department of Chemistry and Chemical Biology, University of New Mexico, Albuquerque, NM 87131, USA. Electronic address: cfeng@unm.edu.

Funding

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
NIGMS NIH HHS R15 GM081811
6 · The paper itself

Abstract

The FMN-heme interdomain electron transfer (IET) in nitric oxide synthase (NOS) is a key stage of the electron transport chain, which supplies the catalytic heme site(s) with the NADPH-derived electrons. While there is a recognition that this IET depends on both the electron tunneling and the conformational dynamics, the detailed mechanism remains unclear. In this work, the IET kinetics were measured by laser flash photolysis for a bidomain oxygenase/FMN (oxyFMN) construct of human inducible NOS (iNOS) over the ionic strength range from 0.1 to 0.5 M. The forward (heme → FMN, k

Indexed as

Electron TransportHemeKineticsNitric Oxide SynthaseOsmolar ConcentrationOxidation-ReductionHemeNitric Oxide SynthaseElectron transferFluorescence lifetimeIonic strengthKineticsLaser flash photolysisNitric oxide synthase

Identifiers

PMID29751215
PMCPMC5983377

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.