ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2008
Copper incorporation into recombinant CotA laccase from Bacillus subtilis: characterization of fully copper loaded enzymes.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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58 citing papers in PubMed, 201 citations in OpenAlex.
- Catalytically active inclusion bodies of Bacillus clausii laccase protein recombinantly produced in E. coli for dye decolorization.Microbial cell factories · 2026Article
- Deciphering Cu(II) EPR in biological buffers: Implications for copper protein studies.Journal of inorganic biochemistry · 2026Article
- Engineering the Bacterial Laccase CotA for Functional Expression and Dye Decolorization Through Site-Directed Mutagenesis.Biology · 2025Article
- Influence of mutations at different distances from the active center on the activity and stability of laccase 13B22.Bioresources and bioprocessing · 2025Article
- Biochemical characterization of a recombinant laccase from Halalkalibacterium halodurans C-125 and its application in the biotransformation of organic compounds.Biotechnology letters · 2024Article
- Plasmid-free production of the plant lignan pinoresinol in growing Escherichia coli cells.Microbial cell factories · 2024Article
- Enhancing catalytic efficiency of Bacillus subtilis laccase BsCotA through active site pocket design.Applied microbiology and biotechnology · 2024Article
- Flexible active-site loops fine-tune substrate specificity of hyperthermophilic metallo-oxidases.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024Article
- Detoxification of aflatoxin B1 by aFrontiers in microbiology · 2024Article
- Phenotypically complex living materials containing engineered cyanobacteria.Nature communications · 2023Article
- Recombinant expression and characterization of a new laccase, bioinformatically identified, from the Antarctic thermophilic bacterium Geobacillus sp. ID17.Extremophiles : life under extreme conditions · 2023Article
- An Inferred Ancestral CotA Laccase with Improved Expression and Kinetic Efficiency.International journal of molecular sciences · 2023Article
- Secretory expression of recombinant small laccase genes in Gram-positive bacteria.Microbial cell factories · 2023Article
- Distal Mutations Shape Substrate-Binding Sites during Evolution of a Metallo-Oxidase into a Laccase.ACS catalysis · 2022Article
- Charged Polypeptide Tail Boosts the Salt Resistance of Enzyme-Containing Complex Coacervate Micelles.Biomacromolecules · 2022Article
- Isothermal titration calorimetric assessment of lignin conversion by laccases.Biotechnology and bioengineering · 2022Article
- MPEPE, a predictive approach to improve protein expression inComputational and structural biotechnology journal · 2022Article
- Copper delivery to an endospore coat protein ofFrontiers in cell and developmental biology · 2022Article
- Decolorization of Textile Dye by Spore Surface Displayed Small Laccase for the Enhanced Thermal Stability and Robust Repeated Reaction.Biotechnology and bioprocess engineering : BBE · 2022Article
- Identification and Characterization of a Novel Plasmid-Encoded Laccase-Like Multicopper Oxidase fromFood technology and biotechnology · 2021Article
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
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Abstract
The copper content of recombinant CotA laccase from Bacillus subtilis produced by Escherichia coli cells is shown to be strongly dependent on the presence of copper and oxygen in the culture media. In copper-supplemented media, a switch from aerobic to microaerobic conditions leads to the synthesis of a recombinant holoenzyme, while the maintenance of aerobic conditions results in the synthesis of a copper-depleted population of proteins. Strikingly, cells grown under microaerobic conditions accumulate up to 80-fold more copper than aerobically grown cells. In vitro copper incorporation into apoenzymes was monitored by optical and electron paramagnetic resonance (EPR) spectroscopy. This analysis reveals that copper incorporation into CotA laccase is a sequential process, with the type 1 copper center being the first to be reconstituted, followed by the type 2 and the type 3 copper centers. The copper reconstitution of holoCotA derivatives depleted in vitro with EDTA results in the complete recovery of the native conformation as monitored by spectroscopic, kinetic and thermal stability analysis. However, the reconstitution of copper to apo forms produced in cultures under aerobic and copper-deficient conditions resulted in incomplete recovery of biochemical properties of the holoenzyme. EPR and resonance Raman data indicate that, presumably, folding in the presence of copper is indispensable for the correct structure of the trinuclear copper-containing site.
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