Evidence map›Paper›PMID 18701448›Full record

ArticleThe Journal of biological chemistry2008

Crystal structures of NADH:FMN oxidoreductase (EmoB) at different stages of catalysis.

Mark S Nissen, Buhyun Youn, Benjamin D Knowles, Jordan W Ballinger, Se-Young Jun, Sara M Belchik, Luying Xun, ChulHee Kang

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.8field-weighted citation impact, top 11% 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

19 citing papers in PubMed, 44 citations in OpenAlex.

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  16. Protein structure determination by exhaustive search of Protein Data Bank derived databases.Proceedings of the National Academy of Sciences of the United States of America · 2010
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  19. Dodecin is the key player in flavin homeostasis of archaea.The Journal of biological chemistry · 2009
    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

8 authors at 1 institution in 1 country.

Mark S NissenSchool of Molecular Biosciences, Washington State University, Pullman, Washington 99164-4660, USA.
Buhyun Youn
Benjamin D Knowles
Jordan W Ballinger
Se-Young Jun
Sara M Belchik
Luying Xun
ChulHee Kang
Washington State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

EDTA has become a major organic pollutant in the environment because of its extreme usage and resistance to biodegradation. Recently, two critical enzymes, EDTA monooxygenase (EmoA) and NADH:FMN oxidoreductase (EmoB), belonging to the newly established two-component flavin-diffusible monooxygenase family, were identified in the EDTA degradation pathway in Mesorhizobium sp. BNC1. EmoA is an FMNH2-dependent enzyme that requires EmoB to provide FMNH2 for the conversion of EDTA to ethylenediaminediacetate. To understand the molecular basis of this FMN-mediated reaction, the crystal structures of the apo-form, FMN.FMN complex, and FMN.NADH complex of EmoB were determined at 2.5 angstroms resolution. The structure of EmoB is a homotetramer consisting of four alpha/beta-single-domain monomers of five parallel beta-strands flanked by five alpha-helices, which is quite different from those of other known two-component flavin-diffusible monooxygenase family members, such as PheA2 and HpaC, in terms of both tertiary and quaternary structures. For the first time, the crystal structures of both the FMN.FMN and FMN.NADH complexes of an NADH:FMN oxidoreductase were determined. Two stacked isoalloxazine rings and nicotinamide/isoalloxazine rings were at a proper distance for hydride transfer. The structures indicated a ping-pong reaction mechanism, which was confirmed by activity assays. Thus, the structural data offer detailed mechanistic information for hydride transfer between NADH to an enzyme-bound FMN and between the bound FMNH2 and a diffusible FMN.

Indexed as

Amino Acid SequenceBacterial ProteinsCatalysisCrystallography, X-RayDimerizationEdetic AcidModels, BiologicalModels, ChemicalModels, MolecularMolecular ConformationMolecular Sequence DataNADH, NADPH OxidoreductasesPhylogenyProtein Structure, QuaternaryProtein Structure, TertiarySequence Homology, Amino AcidBacterial ProteinsEdetic AcidEmoB protein, bacterium BNC1NADH, NADPH Oxidoreductases

Identifiers

PMID18701448
PMCPMC2661417
OpenAlexW2043390112

What OpenQuestion holds

Textmetadata
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.