ArticleFrontiers in bioengineering and biotechnology2015
Biochemical and Structural Properties of a Thermostable Mercuric Ion Reductase from Metallosphaera sedula.
Article in Frontiers in bioengineering and biotechnology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 22 citations in OpenAlex.
- Enzyme Engineering: Performance Optimization, Novel Sources, and Applications in the Food Industry.Foods (Basel, Switzerland) · 2024Review
- Temporal dynamics in a red alga dominated geothermal feature in Yellowstone National Park.ISME communications · 2024Article
- Biochemical and structural basis of mercuric reductase, GbsMerA, from Gelidibacter salicanalis PAMC21136.Scientific reports · 2023Article
- Expanded Diversity and Phylogeny ofFrontiers in microbiology · 2021Article
- 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
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
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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.
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