Evidence map›Paper›PMID 22081476›Full record

ArticleProteins2012

A temperature-dependent conformational change of NADH oxidase from Thermus thermophilus HB8.

Eric D Merkley, Valerie Daggett, William W Parson

Abstract read
In one paragraph

Article in Proteins, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. 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

3 authors.

Eric D MerkleyDepartment of Biochemistry, University of Washington, Seattle, Washington.
Valerie Daggett
William W Parson

Funding

TRAINING IN MOLECULAR BIOPHYSICST32GM008268 · NIGMS · UNIVERSITY OF WASHINGTON · PI KOLLMAN, JUSTIN M, ZHENG, NING · 1988 to 2023
$8.6M
MOLECULAR DYNAMICS SIMULATIONS OF PROTEIN UNFOLDINGR01GM050789 · NIGMS · UNIVERSITY OF WASHINGTON · PI DAGGETT, VALERIE D · 2000 to 2014
$3.9M
MULTI-TIERED PROTEOMIC COMPUTE CLUSTER: PARKINSON'S DISEASES10RR023044 · NCRR · UNIVERSITY OF WASHINGTON · PI GOODLETT, DAVID ROBINSON · 2006 to 2006
$500k
MOLECULAR DYNAMICS SIMULATIONS OF PROTEIN UNFOLDINGR29GM050789 · NIGMS · UNIVERSITY OF WASHINGTON · PI DAGGETT, VALERIE D · 1995 to 1999
–
NCRR NIH HHS 1S10RR023044-01NCRR NIH HHS S10 RR023044NIGMS NIH HHS 5 T32 GM008268-19NIGMS NIH HHS GM 50789NIGMS NIH HHS R01 GM050789NIGMS NIH HHS R29 GM050789NIGMS NIH HHS T32 GM008268
6 · The paper itself

Abstract

Using molecular dynamics simulations and steady-state fluorescence spectroscopy, we have identified a conformational change in the active site of a thermophilic flavoenzyme, NADH oxidase from Thermus thermophilus HB8 (NOX). The enzyme's far-UV circular dichroism spectrum, intrinsic tryptophan fluorescence, and apparent molecular weight measured by dynamic light scattering varied little between 25 and 75°C. However, the fluorescence of the tightly bound FAD cofactor increased approximately fourfold over this temperature range. This effect appears not to be due to aggregation, unfolding, cofactor dissociation, or changes in quaternary structure. We therefore attribute the change in flavin fluorescence to a temperature-dependent conformational change involving the NOX active site. Molecular dynamics simulations and the effects of mutating aromatic residues near the flavin suggest that the change in fluorescence results from a decrease in quenching by electron transfer from tyrosine 137 to the flavin.

Indexed as

Binding SitesCatalytic DomainCircular DichroismFlavin-Adenine DinucleotideLightModels, MolecularMolecular Dynamics SimulationMultienzyme ComplexesMutagenesis, Site-DirectedNADH, NADPH OxidoreductasesProtein ConformationScattering, RadiationSpectrometry, FluorescenceTemperatureThermus thermophilusTryptophanFlavin-Adenine DinucleotideMultienzyme ComplexesNADH, NADPH OxidoreductasesNADH oxidaseTryptophanTyrosineelectron transferflavoproteinsfluorescencefluorescence quenchingmolecular dynamicsNADH oxidasetemperature effectsthermophilesthermophilic enzymesThermus thermophilus

Identifiers

PMID22081476
PMCPMC3288523

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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.