Evidence map›Paper›PMID 27145082›Full record

ArticlePloS one2016

A Hidden Transhydrogen Activity of a FMN-Bound Diaphorase under Anaerobic Conditions.

John Collins, Ting Zhang, Scott Huston, Fangfang Sun, Y-H Percival Zhang, Jinglin Fu

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
1.0field-weighted citation impact, top 22% 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

1 citing paper in PubMed, 11 citations in OpenAlex.

  1. 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.

John CollinsDepartment of Chemistry, Rutgers University-Camden, Camden, New Jersey 08102, United States of America.
Ting ZhangDepartment of Chemistry, Rutgers University-Camden, Camden, New Jersey 08102, United States of America.
Scott HustonDepartment of Chemistry, Rutgers University-Camden, Camden, New Jersey 08102, United States of America.
Fangfang SunCell Free Bioinnovations Inc., Blacksburg, Virginia 24060, United States of America.
Y-H Percival ZhangCell Free Bioinnovations Inc., Blacksburg, Virginia 24060, United States of America.
Jinglin FuDepartment of Chemistry, Rutgers University-Camden, Camden, New Jersey 08102, United States of America.
Rutgers, The State University of New Jersey · USVirginia Tech · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundRedox cofactors of NADH/NADPH participate in many cellular metabolic pathways for facilitating the electron transfer from one molecule to another in redox reactions. Transhydrogenase plays an important role in linking catabolism and anabolism, regulating the ratio of NADH/NADPH in cells. The cytoplasmic transhydrogenases could be useful to engineer synthetic biochemical pathways for the production of high-value chemicals and biofuels. METHODOLOGY/PRINCIPAL

findingsA transhydrogenase activity was discovered for a FMN-bound diaphorase (DI) from Geobacillus stearothermophilus under anaerobic conditions. The DI-catalyzed hydride exchange were monitored and characterized between a NAD(P)H and a thio-modified NAD+ analogue. This new function of DI was demonstrated to transfer a hydride from NADPH to NAD+ that was consumed by NAD-specific lactate dehydrogenase and malic dehydrogenase. CONCLUSIONS/SIGNIFICANCE: We discover a novel transhydrogenase activity of a FMN-DI by stabilizing the reduced state of FMNH2 under anaerobic conditions. FMN-DI was demonstrated to catalyze the hydride transfer between NADPH and NAD+. In the future, it may be possible to incorporate this FMN-DI into synthetic enzymatic pathways for balancing NADH generation and NADPH consumption for anaerobic production of biofuels and biochemicals.

Indexed as

Binding SitesCatalysisDihydrolipoamide DehydrogenaseElectron TransportFlavin MononucleotideGeobacillus stearothermophilusHydroquinonesMalate DehydrogenaseNADNADH DehydrogenaseNADPNADP TranshydrogenasesOxidation-ReductionDihydrolipoamide DehydrogenaseFlavin Mononucleotideflavin mononucleotide hydroquinoneHydroquinonesMalate DehydrogenaseNADNADH DehydrogenaseNADPNADP Transhydrogenases

Identifiers

PMID27145082
PMCPMC4856307
OpenAlexW2346898879

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.