ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2011
Electronic and geometric structures of the organophosphate-degrading enzyme from Agrobacterium radiobacter (OpdA).
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 54 citations in OpenAlex.
- Structural and Functional Insight into the Mechanism of the Fe-S Cluster-Dependent Dehydratase from Paralcaligenes ureilyticus.Chemistry (Weinheim an der Bergstrasse, Germany) · 2023Article
- Overview of a bioremediation tool: organophosphorus hydrolase and its significant application in the food, environmental, and therapy fields.Applied microbiology and biotechnology · 2021Review
- Enzymes, Reacting with Organophosphorus Compounds as Detoxifiers: Diversity and Functions.International journal of molecular sciences · 2021Review
- Structure and mechanism of potent bifunctional β-lactam- and homoserine lactone-degrading enzymes from marine microorganisms.Scientific reports · 2020Article
- Mechanistic Studies of Homo- and Heterodinuclear Zinc Phosphoesterase Mimics: What Has Been Learned?Frontiers in chemistry · 2019Review
- Use of magnetic circular dichroism to study dinuclear metallohydrolases and the corresponding biomimetics.European biophysics journal : EBJ · 2015Review
- Inhibition of the dapE-Encoded N-Succinyl-L,L-diaminopimelic Acid Desuccinylase from Neisseria meningitidis by L-Captopril.Biochemistry · 2015Article
- Comparative investigation of the reaction mechanisms of the organophosphate-degrading phosphotriesterases from Agrobacterium radiobacter (OpdA) and Pseudomonas diminuta (OPH).Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 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
- Identification and characterization of an unusual metallo-β-lactamase from Serratia proteamaculans.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2013Article
- Catalytic mechanisms for phosphotriesterases.Biochimica et biophysica acta · 2013Review
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9 authors at 4 institutions in 3 countries.
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No grant is acknowledged in the PubMed record.
Abstract
The organophosphate-degrading enzyme from Agrobacterium radiobacter (OpdA) is a highly efficient catalyst for the degradation of pesticides and some nerve agents such as sarin. OpdA requires two metal ions for catalytic activity, and hydrolysis is initiated by a nucleophilic hydroxide that is bound to one of these metal ions. The precise location of this nucleophile has been contentious, with both a terminal and a metal-ion-bridging hydroxide as likely candidates. Here, we employed magnetic circular dichroism to probe the electronic and geometric structures of the Co(II)-reconstituted dinuclear metal center in OpdA. In the resting state the metal ion in the more secluded α site is five-coordinate, whereas the Co(II) in the solvent-exposed β site is predominantly six-coordinate with two terminal water ligands. Addition of the slow substrate diethyl 4-methoxyphenyl phosphate does not affect the α site greatly but lowers the coordination number of the β site to five. A reduction in the exchange coupling constant indicates that substrate binding also triggers a shift of the μ-hydroxide into a pseudoterminal position in the coordination sphere of either the α or the β metal ion. Mechanistic implications of these observations are discussed.
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