A novel mercuric reductase from the unique deep brine environment of atlantis II in the red sea

Ahmed Anazadeh Sayed, Mohamed A. Ghazy, Ari José Scattone Ferreira, João Carlos Setúbal, Felipe Santiago Chambergo, Amged Ouf, Mustafa Adel, Adam Sean Dawe, John A.C. Archer, Vladimir B. Bajic, Rania Siam, Hamza A A El-Dorry

Research output: Contribution to journalArticlepeer-review

38 Scopus citations


Aunique 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 Hg2+, and efficiently detoxifies Hg2+ 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. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.
Original languageEnglish (US)
Pages (from-to)1675-1687
Number of pages13
JournalJournal of Biological Chemistry
Issue number3
StatePublished - Nov 26 2013

Bibliographical note

KAUST Repository Item: Exported on 2020-10-01

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology


Dive into the research topics of 'A novel mercuric reductase from the unique deep brine environment of atlantis II in the red sea'. Together they form a unique fingerprint.

Cite this