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Biochemical and Structural Properties of a Thermostable Mercuric Ion Reductase from Metallosphaera sedula
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 t...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4500099/ https://www.ncbi.nlm.nih.gov/pubmed/26217660 http://dx.doi.org/10.3389/fbioe.2015.00097 |
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author | Artz, Jacob H. White, Spencer N. Zadvornyy, Oleg A. Fugate, Corey J. Hicks, Danny Gauss, George H. Posewitz, Matthew C. Boyd, Eric S. Peters, John W. |
author_facet | Artz, Jacob H. White, Spencer N. Zadvornyy, Oleg A. Fugate, Corey J. Hicks, Danny Gauss, George H. Posewitz, Matthew C. Boyd, Eric S. Peters, John W. |
author_sort | Artz, Jacob H. |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-4500099 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-45000992015-07-27 Biochemical and Structural Properties of a Thermostable Mercuric Ion Reductase from Metallosphaera sedula Artz, Jacob H. White, Spencer N. Zadvornyy, Oleg A. Fugate, Corey J. Hicks, Danny Gauss, George H. Posewitz, Matthew C. Boyd, Eric S. Peters, John W. Front Bioeng Biotechnol Bioengineering and Biotechnology 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. Frontiers Media S.A. 2015-07-13 /pmc/articles/PMC4500099/ /pubmed/26217660 http://dx.doi.org/10.3389/fbioe.2015.00097 Text en Copyright © 2015 Artz, White, Zadvornyy, Fugate, Hicks, Gauss, Posewitz, Boyd and Peters. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Bioengineering and Biotechnology Artz, Jacob H. White, Spencer N. Zadvornyy, Oleg A. Fugate, Corey J. Hicks, Danny Gauss, George H. Posewitz, Matthew C. Boyd, Eric S. Peters, John W. Biochemical and Structural Properties of a Thermostable Mercuric Ion Reductase from Metallosphaera sedula |
title | Biochemical and Structural Properties of a Thermostable Mercuric Ion Reductase from Metallosphaera sedula |
title_full | Biochemical and Structural Properties of a Thermostable Mercuric Ion Reductase from Metallosphaera sedula |
title_fullStr | Biochemical and Structural Properties of a Thermostable Mercuric Ion Reductase from Metallosphaera sedula |
title_full_unstemmed | Biochemical and Structural Properties of a Thermostable Mercuric Ion Reductase from Metallosphaera sedula |
title_short | Biochemical and Structural Properties of a Thermostable Mercuric Ion Reductase from Metallosphaera sedula |
title_sort | biochemical and structural properties of a thermostable mercuric ion reductase from metallosphaera sedula |
topic | Bioengineering and Biotechnology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4500099/ https://www.ncbi.nlm.nih.gov/pubmed/26217660 http://dx.doi.org/10.3389/fbioe.2015.00097 |
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