Evidence map›Paper›PMID 23443126›Full record

ArticleInternational journal of molecular sciences2012

Electrochemical characterization of Escherichia coli adaptive response protein AidB.

Michael J Hamill, Marco Jost, Cintyu Wong, Nicholas C Bene, Catherine L Drennan, Sean J Elliott

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 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
0.1field-weighted citation impact, top 47% 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

4 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Article
  3. Characterization of the Proteins Involved in the DNA Repair Mechanism inInternational journal of molecular sciences · 2020
    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

6 authors at 2 institutions in 1 country.

Michael J HamillDepartment of Chemistry, Boston University, 590 Commonwealth Ave., Boston, MA 02215, USA. elliott@bu.edu.
Marco Jost
Cintyu Wong
Nicholas C Bene
Catherine L Drennan
Sean J Elliott
Boston University · USMassachusetts Institute of Technology · US

Funding

TOXICOLOGY CORE UNITP30ES002109 · NIEHS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI LEVINE, STUART S · 1985 to 2020
$25.6M
Complex Metallocluster Structure and AssemblyR01GM069857 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI DRENNAN, CATHERINE L · 2004 to 2017
$3.1M
The Electrochemistry of Diheme Cytochrome c PeroxidasesR01GM072663 · NIGMS · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI ELLIOTT, SEAN J · 2006 to 2010
$1.2M
NIEHS NIH HHS P30 ES002109NIEHS NIH HHS P30-ES002109NIGMS NIH HHS R01 GM069857NIGMS NIH HHS R01 GM072663NIGMS NIH HHS R01-GM072663NIGMS NIH HHS R01-GM69857
6 · The paper itself

Abstract

When exposed to known DNA-damaging alkylating agents, Escherichia coli cells increase production of four DNA repair enzymes: Ada, AlkA, AlkB, and AidB. The role of three enzymes (Ada, AlkA, and AlkB) in repairing DNA lesions has been well characterized, while the function of AidB is poorly understood. AidB has a distinct cofactor that is potentially related to the elusive role of AidB in adaptive response: a redox active flavin adenine dinucleotide (FAD). In this study, we report the thermodynamic redox properties of the AidB flavin for the first time, both for free protein and in the presence of potential substrates. We find that the midpoint reduction potential of the AidB flavin is within a biologically relevant window for redox chemistry at -181 mV, that AidB significantly stabilizes the flavin semiquinone, and that small molecule binding perturbs the observed reduction potential. Our electrochemical results combined with structural analysis allow for fresh comparisons between AidB and the homologous acyl-coenzyme A dehydrogenase (ACAD) family of enzymes. AidB exhibits several discrepancies from ACADs that suggest a novel catalytic mechanism distinct from that of the ACAD family enzymes.

Indexed as

DNA RepairElectrochemical TechniquesEscherichia coliEscherichia coli ProteinsFlavin-Adenine DinucleotideThermodynamicsAidB protein, E coliEscherichia coli ProteinsFlavin-Adenine Dinucleotide

Identifiers

PMID23443126
PMCPMC3546729
OpenAlexW2115378356

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.