ArticleThe Biochemical journal2006
Anomalous scattering analysis of Agrobacterium radiobacter phosphotriesterase: the prominent role of iron in the heterobinuclear active site.
Article in The Biochemical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 59 citations in OpenAlex.
- Applications of Microbial Organophosphate-Degrading Enzymes to Detoxification of Organophosphorous Compounds for Medical Countermeasures against Poisoning and Environmental Remediation.International journal of molecular sciences · 2024Review
- Overview of a bioremediation tool: organophosphorus hydrolase and its significant application in the food, environmental, and therapy fields.Applied microbiology and biotechnology · 2021Review
- Efficacy of an organophosphorus hydrolase enzyme (OpdA) in human serum and minipig models of organophosphorus insecticide poisoning.Clinical toxicology (Philadelphia, Pa.) · 2020Article
- Rational engineering of a native hyperthermostable lactonase into a broad spectrum phosphotriesterase.Scientific reports · 2017Article
- Evolutionary expansion of the amidohydrolase superfamily in bacteria in response to the synthetic compounds molinate and diuron.Applied and environmental microbiology · 2015Article
- 300-Fold increase in production of the Zn2+-dependent dechlorinase TrzN in soluble form via apoenzyme stabilization.Applied and environmental microbiology · 2014Article
- Determination of the catalytic activity of binuclear metallohydrolases using isothermal titration calorimetry.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
- A 5000-fold increase in the specificity of a bacterial phosphotriesterase for malathion through combinatorial active site mutagenesis.PloS one · 2014Article
- The effect of conformational variability of phosphotriesterase upon N-acyl-L-homoserine lactone and paraoxon binding: insights from molecular dynamics studies.Molecules (Basel, Switzerland) · 2013Article
- Crystallization and preliminary X-ray diffraction analysis of the lactonase VmoLac from Vulcanisaeta moutnovskia.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Crystallization and preliminary X-ray diffraction analysis of the organophosphorus hydrolase OPHC2 from Pseudomonas pseudoalcaligenes.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Structural and enzymatic characterization of the phosphotriesterase OPHC2 from Pseudomonas pseudoalcaligenes.PloS one · 2013Article
- Diminishing returns and tradeoffs constrain the laboratory optimization of an enzyme.Nature communications · 2012Article
- Structural and enzymatic characterization of the lactonase SisLac from Sulfolobus islandicus.PloS one · 2012Article
- Characterisation of the organophosphate hydrolase catalytic activity of SsoPox.Scientific reports · 2012Article
- Gulosibacter molinativorax ON4T molinate hydrolase, a novel cobalt-dependent amidohydrolase.Journal of bacteriology · 2011Article
- Conformational sampling, catalysis, and evolution of the bacterial phosphotriesterase.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Combining structure and dynamics: non-denaturing high-pressure effect on lysozyme in solution.Journal of the Royal Society, Interface · 2009Article
- Structure-based rational design of a phosphotriesterase.Applied and environmental microbiology · 2009Article
- Substrate-promoted formation of a catalytically competent binuclear center and regulation of reactivity in a glycerophosphodiesterase from Enterobacter aerogenes.Journal of the American Chemical Society · 2008Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial phosphotriesterases are binuclear metalloproteins for which the catalytic mechanism has been studied with a variety of techniques, principally using active sites reconstituted in vitro from apoenzymes. Here, atomic absorption spectroscopy and anomalous X-ray scattering have been used to determine the identity of the metals incorporated into the active site in vivo. We have recombinantly expressed the phosphotriesterase from Agrobacterium radiobacter (OpdA) in Escherichia coli grown in medium supplemented with 1 mM CoCl2 and in unsupplemented medium. Anomalous scattering data, collected from a single crystal at the Fe-K, Co-K and Zn-K edges, indicate that iron and cobalt are the primary constituents of the two metal-binding sites in the catalytic centre (alpha and beta) in the protein expressed in E. coli grown in supplemented medium. Comparison with OpdA expressed in unsupplemented medium demonstrates that the cobalt present in the supplemented medium replaced zinc at the beta-position of the active site, which results in an increase in the catalytic efficiency of the enzyme. These results suggest an essential role for iron in the catalytic mechanism of bacterial phosphotriesterases, and that these phosphotriesterases are natively heterobinuclear iron-zinc enzymes.
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