Evidence map›Paper›PMID 21923139›Full record

ArticleBiochemistry2011

Variations in protein-flavin hydrogen bonding in a light, oxygen, voltage domain produce non-Arrhenius kinetics of adduct decay.

Brian D Zoltowski, Abigail I Nash, Kevin H Gardner

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
5.3field-weighted citation impact, top 5% 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

26 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
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  4. Article
  5. A structural decryption of cryptochromes.Frontiers in chemistry · 2024
    Review
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  10. Article
  11. Toward Multiplexed Optogenetic Circuits.Frontiers in bioengineering and biotechnology · 2021
    Review
  12. Tunable Properties of Nature-InspiredMolecules (Basel, Switzerland) · 2020
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  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

3 authors at 1 institution in 1 country.

Brian D ZoltowskiDepartment of Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas 75390-8816, USA.
Abigail I Nash
Kevin H Gardner
The University of Texas Southwestern Medical Center · US

Funding

Molecular Biophysics Predoctoral Training ProgramT32GM008297 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI CHOOK, YUH MIN · 1989 to 2018
$2.4M
Structural studies of PAS domain signaling mechanismsR01GM081875 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI GARDNER, KEVIN H · 2007 to 2010
$1.2M
Structural Dynamics of Pas Domain Containing Transcription FactorsF32GM090671 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI ZOLTOWSKI, BRIAN DAVID · 2010 to 2011
$77k
NIGMS NIH HHS F32 GM090671NIGMS NIH HHS R01 GM081875NIGMS NIH HHS T32 GM008297
6 · The paper itself

Abstract

Light, oxygen, voltage (LOV) domains utilize a conserved blue light-dependent mechanism to control a diverse array of effector domains in biological and engineered proteins. Variations in the kinetics and efficiency of LOV photochemistry fine-tune various aspects of the photic response. Characterization of the kinetics of a key aspect of this photochemical mechanism in EL222, a blue light responsive DNA binding protein from Erythrobacter litoralis HTCC2594, reveals unique non-Arrhenius behavior in the rate of dark-state cleavage of the photochemically generated adduct. Sequence analysis and mutagenesis studies establish that this effect stems from a Gln to Ala mutation unique to EL222 and homologous proteins from marine bacteria. Kinetic and spectroscopic analyses reveal that hydrogen bonding interactions between the FMN N1, O2, and ribityl hydroxyls and the surrounding protein regulate photocycle kinetics and stabilize the LOV active site from temperature-induced alteration in local structure. Substitution of residues interacting with the N1-O2 locus modulates adduct stability, structural flexibility, and sequestration of the active site from bulk solvent without perturbation of light-activated DNA binding. Together, these variants link non-Arrhenius behavior to specific alteration of an H-bonding network, while affording tunability of photocycle kinetics.

Indexed as

AlanineBacterial ProteinsBiochemistryCatalytic DomainGenetic VariationGlutamineHydrogen BondingKineticsMutagenesisOxygenPhotochemistryProtein Structure, TertiarySphingomonadaceaeTemperatureAlanineBacterial ProteinsGlutamineOxygen

Identifiers

PMID21923139
PMCPMC3381950
OpenAlexW317852650

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.