Evidence map›Paper›PMID 26477677›Full record

ArticleThe journal of physical chemistry. A2015

Solving Kinetic Equations for the Laser Flash Photolysis Experiment on Nitric Oxide Synthases: Effect of Conformational Dynamics on the Interdomain Electron Transfer.

Andrei V Astashkin, Changjian Feng

Abstract read
In one paragraph

Article in The journal of physical chemistry. A, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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.

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3 · Its place in the literature

Who cites it

10 citing papers in PubMed.

  1. Detection of a clamp-shaped conformation of a neuronal nitric oxide synthase construct by pulsed EPR.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025
    Article
  2. 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
    Article
  3. Article
  4. 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
  5. Article
  6. Article
  7. 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
  8. Article
  9. Review
  10. Article
4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

2 authors.

Andrei V AstashkinDepartment of Chemistry and Biochemistry, University of Arizona , Tucson, Arizona 85721, United States.
Changjian FengDepartment of Pharmaceutical Sciences, College of Pharmacy, University of New Mexico , Albuquerque, New Mexico 87131, United States.

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 GM081811,NIGMS NIH HHS R15 GM081811
6 · The paper itself

Abstract

The production of nitric oxide by the nitric oxide synthase (NOS) enzyme depends on the interdomain electron transfer (IET) between the flavin mononucleotide (FMN) and heme domains. Although the rate of this IET has been measured by laser flash photolysis (LFP) for various NOS proteins, no rigorous analysis of the relevant kinetic equations was performed so far. In this work, we provide an analytical solution of the kinetic equations underlying the LFP approach. The derived expressions reveal that the bulk IET rate is significantly affected by the conformational dynamics that determines the formation and dissociation rates of the docking complex between the FMN and heme domains. We show that in order to informatively study the electron transfer across the NOS enzyme, LFP should be used in combination with other spectroscopic methods that could directly probe the docking equilibrium and the conformational change rate constants. The implications of the obtained analytical expressions for the interpretation of the LFP results from various native and modified NOS proteins are discussed. The mathematical formulas derived in this work should also be applicable for interpreting the IET kinetics in other modular redox enzymes.

Indexed as

ElectronsPhotolysisAnimalsCarbon MonoxideHemeHumansKineticsLasersMiceMutationNitric OxideNitric Oxide SynthaseProtein ConformationRatsCarbon MonoxideHemeNitric OxideNitric Oxide Synthase

Identifiers

PMID26477677
PMCPMC5518706

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Registered trials

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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.