Evidence map›Paper›PMID 23086017›Full record

ReviewDalton transactions (Cambridge, England : 2003)2013

MauG: a di-heme enzyme required for methylamine dehydrogenase maturation.

Carrie M Wilmot, Erik T Yukl

Open access · greenAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Dalton transactions (Cambridge, England : 2003), 2013. 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
0.5field-weighted citation impact, top 33% 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, 10 citations in OpenAlex.

  1. Metals and Methanotrophy.Applied and environmental microbiology · 2018
    Review
  2. Article
  3. Heme enzyme structure and function.Chemical reviews · 2014
    Review
  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

2 authors at 1 institution in 1 country.

Carrie M WilmotDepartment of Biochemistry, Molecular Biology and Biophysics, Minneapolis, Minnesota 55455, USA. wilmo004@umn.edu
Erik T Yukl
University of Minnesota · US

Funding

Catalysis and biogenesis in methylamine dehydrogenaseR01GM066569 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI WILMOT, CAROLINE MARY · 2002 to 2015
$4.0M
MauG-preMADH intermediate structures: Insight into long range electron transferF32GM097779 · NIGMS · UNIVERSITY OF MINNESOTA · PI YUKL, ERIK T · 2011 to 2013
$112k
NIGMS NIH HHS F32 GM097779NIGMS NIH HHS GM-66569NIGMS NIH HHS GM-97779NIGMS NIH HHS R01 GM066569
6 · The paper itself

Abstract

Methylamine dehydrogenase (MADH) requires the cofactor tryptophan tryptophylquinone (TTQ) for activity. TTQ is a posttranslational modification that results from an 8-electron oxidation of two specific tryptophans in the MADH β-subunit. The final 6-electron oxidation is catalyzed by an unusual c-type di-heme enzyme, MauG. The di-ferric enzyme can react with H(2)O(2), but atypically for c-type hemes the di-ferrous enzyme can react with O(2) as well. In both cases, an unprecedented bis-Fe(IV) redox state is formed, composed of a ferryl heme (Fe(IV)=O) with the second heme as Fe(IV) stabilized by His-Tyr axial ligation. Bis-Fe(IV) MauG acts as a potent 2-electron oxidant. Catalysis is long-range and requires a hole hopping electron transfer mechanism. This review highlights the current knowledge and focus of research into this fascinating system.

Indexed as

HemeCrystallography, X-RayElectron TransportEndopeptidasesIndolequinonesOxidoreductases Acting on CH-NH Group DonorsTryptophanBacillus polymyxa proteinaseEndopeptidasesHemeIndolequinonesmethylamine dehydrogenaseOxidoreductases Acting on CH-NH Group DonorsTryptophantryptophan tryptophylquinone

Identifiers

PMID23086017
PMCPMC3566329
OpenAlexW2146362011

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.