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dc.contributor.authorSayed, Ahmed Anazadeh
dc.contributor.authorGhazy, Mohamed A.
dc.contributor.authorFerreira, Ari José Scattone
dc.contributor.authorSetúbal, João Carlos
dc.contributor.authorChambergo, Felipe Santiago
dc.contributor.authorOuf, Amged
dc.contributor.authorAdel, Mustafa
dc.contributor.authorDawe, Adam Sean
dc.contributor.authorArcher, John A.C.
dc.contributor.authorBajic, Vladimir B.
dc.contributor.authorSiam, Rania
dc.contributor.authorEl-Dorry, Hamza A A
dc.date.accessioned2015-08-03T11:35:55Z
dc.date.available2015-08-03T11:35:55Z
dc.date.issued2013-11-26
dc.identifier.citationSayed, A., Ghazy, M. A., Ferreira, A. J. S., Setubal, J. C., Chambergo, F. S., Ouf, A., … El-Dorry, H. (2013). A Novel Mercuric Reductase from the Unique Deep Brine Environment of Atlantis II in the Red Sea. Journal of Biological Chemistry, 289(3), 1675–1687. doi:10.1074/jbc.m113.493429
dc.identifier.issn00219258
dc.identifier.pmid24280218
dc.identifier.doi10.1074/jbc.M113.493429
dc.identifier.urihttp://hdl.handle.net/10754/563106
dc.description.abstractAunique 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.
dc.publisherAmerican Society for Biochemistry & Molecular Biology (ASBMB)
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3894346
dc.titleA novel mercuric reductase from the unique deep brine environment of atlantis II in the red sea
dc.typeArticle
dc.contributor.departmentComputational Bioscience Research Center (CBRC)
dc.contributor.departmentComputer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division
dc.contributor.departmentApplied Mathematics and Computational Science Program
dc.contributor.departmentOffice of the VP
dc.identifier.journalJournal of Biological Chemistry
dc.identifier.pmcidPMC3894346
dc.contributor.institutionDepartment of Biology and the Science and Technology Research Center, School of Sciences and Engineering, American University in Cairo, AUC Avenue, P. O. Box 74, New Cairo 11835, Egypt
dc.contributor.institutionDepartamento de Bioquímica, Instituto de Química, Universidade de São Paulo, Avenida Prof. Lineu Prestes, 748, São Paulo, SP 05508-000, Brazil
dc.contributor.institutionEscola de Artes, Ciências e Humanidades, Universidade de São Paulo, Avenida Arlindo Bettio 1000, São Paulo, SP 03828-000, Brazil
kaust.personDawe, Adam Sean
kaust.personArcher, John A.C.
kaust.personBajic, Vladimir B.
dc.date.published-online2013-11-26
dc.date.published-print2014-01-17


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