Evidence map›Paper›PMID 35877011›Full record

ArticleWorld journal of microbiology & biotechnology2022

Homology modeling and virtual characterization of cytochrome c nitrite reductase (NrfA) in three model bacteria responsible for short-circuit pathway, DNRA in the terrestrial nitrogen cycle.

Megha Kaviraj, Upendra Kumar, A K Nayak, Soumendranath Chatterjee

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Article in World journal of microbiology & biotechnology, 2022. 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
0.5field-weighted citation impact, top 39% of its field
1 · What the graph read from it

What it found

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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.

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3 · Its place in the literature

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1 citing paper in PubMed, 6 citations in OpenAlex.

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4 · The record

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5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Megha KavirajICAR- National Rice Research Institute, Cuttack, Odisha, 753006, India. meghakaviraj31@gmail.com.
Upendra KumarICAR- National Rice Research Institute, Cuttack, Odisha, 753006, India. ukumarmb@gmail.com.
A K NayakICAR- National Rice Research Institute, Cuttack, Odisha, 753006, India.
Soumendranath ChatterjeeThe University of Burdwan, Burdwan, West Bengal, 713104, India.
Central Rice Research Institute · INUniversity of Burdwan · IN

Funding

Indian Council of Agricultural Research EAP 200 and EAP 275
6 · The paper itself

Abstract

NrfA is the molecular marker for dissimilatory nitrate reduction to ammonium (DNRA) activity, catalysing cytochrome c nitrite reductase enzyme. However, the limited study has been made so far to understand the structural homology modeling of NrfA protein in DNRA bacteria. Therefore, three model DNRA bacteria (Escherechia coli, Wolinella succinogenes and Shewanella oneidensis) were chosen in this study for in-silico protein modeling of NrfA which roughly consists of similar length of amino acids and molecular weight and they belong to two contrasting taxonomic families (γ-proteobacteria with nrfABCDEFG and ε-proteobacteria with nrfHAIJ operon). Multiple bioinformatic tools were used to examine the primary, secondary, and tertiary structure of NrfA protein using three distinct homology modeling pipelines viz., Phyre2, Swiss model and Modeller. The results indicated that NrfA protein in E. coli, W. succinogenes and S. oneidensis was mostly periplasmic and hydrophilic. Four conserved Cys-X1-X2-Cys-His motifs, one Cys-X1-X2-Cys-Lys haem-binding motif and Ca ligand were also identified in NrfA protein irrespective of three model bacteria. Moreover, 11 identical conserved amino acids sequence was observed for the first time between serine and proline in NrfA protein. Secondary structure of NrfA revealed that α-helices were observed in 77.9%, 73.4%, and 77.4% in E. coli, W. succinogenes and S. oneidensis, respectively. Ramachandran plot showed that number of residue in favored region in E. coli, W. succinogenes and S. oneidensis was 97.03%, 97.01% and 97.25%, respectively. Our findings also revealed that among three pipelines, Modeller was considered the best in-silico tool for prediction of NrfA protein. Overall, significant findings of this study may aid in the identification of future unexplored DNRA bacteria containing cytochrome c nitrite reductase. The NrfA system, which is linked to respiratory nitrite ammonification, provides an analogous target for monitoring less studied N-retention processes, particularly in agricultural ecosystems. Furthermore, one of the challenging research tasks for the future is to determine how the NrfA protein responds to redox status in the microbial cells.

Indexed as

Ammonium CompoundsNitratesAmino AcidsBacteriaCytochromes a1Cytochromes c1EcosystemEscherichia coliHumansNitrate ReductasesNitrite ReductasesNitrogen CycleAmino AcidsAmmonium CompoundsCytochromes a1Cytochromes c1nitrate reductase (cytochrome)Nitrate ReductasesNitratesNitrite ReductasesDNRAHomology protein modelingIn-silico analysisNrfA proteinRamachandran plot

Identifiers

PMID35877011
OpenAlexW4287147590

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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.