ArticleThe Journal of biological chemistry2014
A novel mercuric reductase from the unique deep brine environment of Atlantis II in the Red Sea.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 43 citations in OpenAlex.
- Metagenomic profiling of antibiotic resistance genes in Red Sea brine pools.Archives of microbiology · 2023Article
- Evaluation of a Thermophilic, Psychrostable, and Heavy Metal-Resistant Red Sea Brine Pool Esterase.Marine drugs · 2022Article
- Perspectives on the microorganism of extreme environments and their applications.Current research in microbial sciences · 2022Review
- Industrial Biotechnology Based on Enzymes From Extreme Environments.Frontiers in bioengineering and biotechnology · 2022Review
- Expanded Diversity and Phylogeny ofFrontiers in microbiology · 2021Article
- Novel Enzymes From the Red Sea Brine Pools: Current State and Potential.Frontiers in microbiology · 2021Review
- Bioprospecting of Novel Extremozymes From Prokaryotes-The Advent of Culture-Independent Methods.Frontiers in microbiology · 2021Review
- Deep Hypersaline Anoxic Basins as Untapped Reservoir of Polyextremophilic Prokaryotes of Biotechnological Interest.Marine drugs · 2020Review
- Toxicomicrobiomics: The Human Microbiome vs. Pharmaceutical, Dietary, and Environmental Xenobiotics.Frontiers in pharmacology · 2020Review
- Properties and Applications of Extremozymes from Deep-Sea Extremophilic Microorganisms: A Mini Review.Marine drugs · 2019Review
- Molecular Adaptations of Bacterial Mercuric Reductase to the Hypersaline Kebrit Deep in the Red Sea.Applied and environmental microbiology · 2019Article
- Thermal Stability of a Mercuric Reductase from the Red Sea Atlantis II Hot Brine Environment as Analyzed by Site-Directed Mutagenesis.Applied and environmental microbiology · 2019Article
- A novel thermostable and halophilic thioredoxin reductase from the Red Sea Atlantis II hot brine pool.PloS one · 2019Article
- Modulation of the flavin-protein interactions in NADH peroxidase and mercuric ion reductase: a resonance Raman study.European biophysics journal : EBJ · 2018Article
- Antibiotic resistance in the most unlikeliest of places.Microbial biotechnology · 2017Article
- Building a bio-based industry in the Middle East through harnessing the potential of the Red Sea biodiversity.Applied microbiology and biotechnology · 2017Review
- Novel thermostable antibiotic resistance enzymes from the Atlantis II Deep Red Sea brine pool.Microbial biotechnology · 2017Article
- Red Sea Atlantis II brine pool nitrilase with unique thermostability profile and heavy metal tolerance.BMC biotechnology · 2016Article
- Rapid Bioinformatic Identification of Thermostabilizing Mutations.Biophysical journal · 2015Article
- Biochemical and Structural Properties of a Thermostable Mercuric Ion Reductase from Metallosphaera sedula.Frontiers in bioengineering and biotechnology · 2015Article
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Authors and funding
12 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A unique combination of physicochemical conditions prevails in the lower convective layer (LCL) of the brine pool at Atlantis II (ATII) Deep in the Red Sea. With a maximum depth of over 2000 m, the pool is characterized by acidic pH (5.3), high temperature (68 °C), salinity (26%), low light levels, anoxia, and high concentrations of heavy metals. We have established a metagenomic dataset derived from the microbial community in the LCL, and here we describe a gene for a novel mercuric reductase, a key component of the bacterial detoxification system for mercuric and organomercurial species. The metagenome-derived gene and an ortholog from an uncultured soil bacterium were synthesized and expressed in Escherichia coli. The properties of their products show that, in contrast to the soil enzyme, the ATII-LCL mercuric reductase is functional in high salt, stable at high temperatures, resistant to high concentrations of Hg(2+), and efficiently detoxifies Hg(2+) in vivo. Interestingly, despite the marked functional differences between the orthologs, their amino acid sequences differ by less than 10%. Site-directed mutagenesis and kinetic analysis of the mutant enzymes, in conjunction with three-dimensional modeling, have identified distinct structural features that contribute to extreme halophilicity, thermostability, and high detoxification capacity, suggesting that these were acquired independently during the evolution of this enzyme. Thus, our work provides fundamental structural insights into a novel protein that has undergone multiple biochemical and biophysical adaptations to promote the survival of microorganisms that reside in the extremely demanding environment of the ATII-LCL.
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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.