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Artz JH, White SN, Zadvornyy OA, et al. Biochemical and Structural Properties of a Thermostable Mercuric Ion Reductase from Metallosphaera sedula. Front Bioeng Biotechnol. 2015;3:97doi: 10.3389/fbioe.2015.00097.
Artz, J. H., White, S. N., Zadvornyy, O. A., Fugate, C. J., Hicks, D., Gauss, G. H., Posewitz, M. C., Boyd, E. S., & Peters, J. W. (2015). Biochemical and Structural Properties of a Thermostable Mercuric Ion Reductase from Metallosphaera sedula. Frontiers in bioengineering and biotechnology, 397. https://doi.org/10.3389/fbioe.2015.00097
Artz, Jacob H, et al. "Biochemical and Structural Properties of a Thermostable Mercuric Ion Reductase from Metallosphaera sedula." Frontiers in bioengineering and biotechnology vol. 3 (2015): 97. doi: https://doi.org/10.3389/fbioe.2015.00097
Artz JH, White SN, Zadvornyy OA, Fugate CJ, Hicks D, Gauss GH, Posewitz MC, Boyd ES, Peters JW. Biochemical and Structural Properties of a Thermostable Mercuric Ion Reductase from Metallosphaera sedula. Front Bioeng Biotechnol. 2015 Jul 13;3:97. doi: 10.3389/fbioe.2015.00097. eCollection 2015. PMID: 26217660; PMCID: PMC4500099.
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Front Bioeng Biotechnol. 2015 Jul 13;3:97. doi: 10.3389/fbioe.2015.00097. eCollection 2015.

Biochemical and Structural Properties of a Thermostable Mercuric Ion Reductase from Metallosphaera sedula.

Frontiers in bioengineering and biotechnology

Jacob H Artz, Spencer N White, Oleg A Zadvornyy, Corey J Fugate, Danny Hicks, George H Gauss, Matthew C Posewitz, Eric S Boyd, John W Peters

Affiliations

  1. Department of Chemistry and Biochemistry, Montana State University , Bozeman, MT , USA.
  2. Department of Chemistry and Geochemistry, Colorado School of Mines , Golden, CO , USA.
  3. Department of Microbiology and Immunology, Montana State University , Bozeman, MT , USA ; Thermal Biology Institute, Montana State University , Bozeman, MT , USA.

PMID: 26217660 PMCID: PMC4500099 DOI: 10.3389/fbioe.2015.00097

Abstract

Mercuric ion reductase (MerA), a mercury detoxification enzyme, has been tuned by evolution to have high specificity for mercuric ions (Hg(2+)) and to catalyze their reduction to a more volatile, less toxic elemental form. Here, we present a biochemical and structural characterization of MerA from the thermophilic crenarchaeon Metallosphaera sedula. MerA from M. sedula is a thermostable enzyme, and remains active after extended incubation at 97°C. At 37°C, the NADPH oxidation-linked Hg(2+) reduction specific activity was found to be 1.9 μmol/min⋅mg, increasing to 3.1 μmol/min⋅mg at 70°C. M. sedula MerA crystals were obtained and the structure was solved to 1.6 Å, representing the first solved crystal structure of a thermophilic MerA. Comparison of both the crystal structure and amino acid sequence of MerA from M. sedula to mesophillic counterparts provides new insights into the structural determinants that underpin the thermal stability of the enzyme.

Keywords: MerA; biosensor; mercuric reductase; mercury detoxification; structure; thermophile; thermostability

References

  1. Structure. 2000 May 15;8(5):493-504 - PubMed
  2. FEMS Microbiol Rev. 2000 Dec;24(5):615-23 - PubMed
  3. Biosens Bioelectron. 2001 Jan;16(1-2):9-16 - PubMed
  4. Nucleic Acids Res. 2003 Jul 1;31(13):3316-9 - PubMed
  5. FEMS Microbiol Rev. 2003 Jun;27(2-3):313-39 - PubMed
  6. FEMS Microbiol Rev. 2003 Jun;27(2-3):355-84 - PubMed
  7. Genet Mol Res. 2003 Mar 31;2(1):92-101 - PubMed
  8. Microb Ecol. 2003 Nov;46(4):429-41 - PubMed
  9. J Bacteriol. 2004 Jan;186(2):427-37 - PubMed
  10. Prog Nucleic Acid Res Mol Biol. 2004;78:89-142 - PubMed
  11. J Comput Chem. 2004 Oct;25(13):1605-12 - PubMed
  12. Acta Crystallogr D Biol Crystallogr. 1997 May 1;53(Pt 3):240-55 - PubMed
  13. Appl Environ Microbiol. 2005 Jan;71(1):220-6 - PubMed
  14. Biochemistry. 2005 Aug 30;44(34):11402-16 - PubMed
  15. Appl Environ Microbiol. 2005 Dec;71(12):8836-45 - PubMed
  16. Bioinformatics. 2007 Nov 1;23(21):2947-8 - PubMed
  17. Appl Environ Microbiol. 2008 Feb;74(3):682-92 - PubMed
  18. Curr Opin Biotechnol. 2008 Oct;19(5):445-53 - PubMed
  19. Environ Microbiol. 2009 Apr;11(4):950-9 - PubMed
  20. Acta Crystallogr D Biol Crystallogr. 2010 Jan;66(Pt 1):12-21 - PubMed
  21. Acta Crystallogr D Biol Crystallogr. 2010 Apr;66(Pt 4):486-501 - PubMed
  22. Syst Biol. 2010 May;59(3):307-21 - PubMed
  23. Environ Microbiol. 2010 Nov;12(11):2904-17 - PubMed
  24. Nature. 1991 Jul 11;352(6331):168-72 - PubMed
  25. Biosens Bioelectron. 2011 Mar 15;26(7):3320-4 - PubMed
  26. Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):233-4 - PubMed
  27. Microb Ecol. 2011 Nov;62(4):739-52 - PubMed
  28. Front Microbiol. 2012 Oct 08;3:349 - PubMed
  29. Microbiology. 2013 Jun;159(Pt 6):1198-208 - PubMed
  30. Nucleic Acids Res. 2013 Jul;41(Web Server issue):W597-600 - PubMed
  31. Mol Biol Evol. 2013 Dec;30(12):2725-9 - PubMed
  32. J Biol Chem. 2014 Jan 17;289(3):1675-87 - PubMed
  33. Biochemistry. 2014 Nov 25;53(46):7211-22 - PubMed
  34. Methods Enzymol. 1997;276:307-26 - PubMed
  35. Gene. 1985;34(2-3):253-62 - PubMed
  36. J Biol Chem. 1978 Jun 25;253(12):4341-9 - PubMed
  37. J Gen Microbiol. 1985 May;131(5):1053-9 - PubMed
  38. J Biol Chem. 1982 Mar 10;257(5):2498-503 - PubMed
  39. J Biochem. 1980 Dec;88(6):1895-8 - PubMed
  40. FEBS Lett. 1994 Dec 5;355(3):220-2 - PubMed

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