cota palaestina/oxidase

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Bilirubin oxidase activity of Bacillus subtilis CotA.

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The spore coat protein CotA from Bacillus subtilis was previously identified as a laccase. We have now found that CotA also shows strong bilirubin oxidase activity and markedly higher affinity for bilirubin than conventional bilirubin oxidase. This is the first characterization of bilirubin oxidase

The Pathway for O2 Diffusion inside CotA Laccase and Possible Implications on the Multicopper Oxidases Family.

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Laccases and multicopper oxidases (MCOs) oxidize a wide range of organic compounds while reducing O2 to water, enabling numerous biotechnological applications. It is still unknown how O2 reaches the internalized catalytic center of MCOs where it gets reduced, despite a proposed channel inferred from

Magnetic Ganoderma lucidum spore microspheres: A novel material to immobilize CotA multicopper oxidase for dye decolorization.

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In this study, hollow microspheres were obtained from Ganoderma lucidum spores. Then the hollow microspheres were loaded with Fe3O4 nanoparticles to prepare novel magnetic spore microspheres. TEM images and X-ray diffractometry demonstrated that the Fe3O4 nanoparticles were incorporated throughout

CotA laccase, a novel aflatoxin oxidase from Bacillus licheniformis, transforms aflatoxin B1 to aflatoxin Q1 and epi-aflatoxin Q1.

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In the present study, the CotA protein from Bacillus licheniformis ANSB821 was cloned and expressed in Escherichia coli. Apart from the laccase activities, we found that the recombinant CotA could effectively oxidize aflatoxin B₁ in the absence of redox mediators. The K_m,

CotA, a multicopper oxidase from Bacillus pumilus WH4, exhibits manganese-oxidase activity.

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Multicopper oxidases (MCOs) are a family of enzymes that use copper ions as cofactors to oxidize various substrates. Previous research has demonstrated that several MCOs such as MnxG, MofA and MoxA can act as putative Mn(II) oxidases. Meanwhile, the endospore coat protein CotA from Bacillus species

The role of Glu498 in the dioxygen reactivity of CotA-laccase from Bacillus subtilis.

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The multicopper oxidases couple the one-electron oxidation of four substrate molecules to the four electron reductive cleavage of the O-O bond of dioxygen. This reduction takes place at the trinuclear copper centre of the enzyme and the dioxygen approaches this centre through an entrance channel. In

A simple strategy for extracellular production of CotA laccase in Escherichia coli and decolorization of simulated textile effluent by recombinant laccase.

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Laccases are green oxidases with a number of potential industrial applications. In this study, recombinant Bacillus subtilis CotA laccase was secreted by Escherichia coli via both the α-hemolysin secretion system and the YebF secretion system after microaerobic induction. Meanwhile, we discovered a

Unfolding pathway of CotA-laccase and the role of copper on the prevention of refolding through aggregation of the unfolded state.

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Copper is a redox-active metal and the main player in electron transfer reactions occurring in multicopper oxidases. The role of copper in the unfolding pathway and refolding of the multicopper oxidase CotA laccase in vitro was solved using double-jump stopped-flow experiments. Unfolding of apo- and

Spore-coat laccase CotA from Bacillus subtilis: crystallization and preliminary X-ray characterization by the MAD method.

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Bacterial endospores are highly resistant structures that allow survival for long periods of time in adverse environments. The spore-forming Gram-positive bacterium Bacillus subtilis synthesizes a coat around the endospore during development composed of several assembled polypeptides. The role of

The role of Asp116 in the reductive cleavage of dioxygen to water in CotA laccase: assistance during the proton-transfer mechanism.

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Multi-copper oxidases constitute a family of proteins that are capable of coupling the one-electron oxidation of four substrate equivalents to the four-electron reduction of dioxygen to two molecules of water. The main catalytic stages occurring during the process have already been identified, but

The kinetic role of carboxylate residues in the proximity of the trinuclear centre in the O2 reactivity of CotA-laccase.

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Multicopper oxidases catalyze the four-electron reduction of dioxygen to water without the release of any reactive oxygen intermediate species. The role of carboxylate residue Asp116 located at the exit channel for water molecules of CotA-laccase has been investigated by site-saturation mutagenesis.

The 52 degrees-55 degrees segment of the Bacillus subtilis chromosome: a region devoted to purine uptake and metabolism, and containing the genes cotA, gabP and guaA and the pur gene cluster within a 34960 bp nucleotide sequence.

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Within the framework of the international project for sequencing the entire Bacillus subtilis genome, we have determined the complete sequence of the segment flanking the purE-D gene cluster (55 degrees) as far as cotA (52 degrees). This segment (34960 bp) contains, as well as 12 genes already

Hydrogen Peroxide-Resistant CotA and YjqC of Bacillus altitudinis Spores Are a Promising Biocatalyst for Catalyzing Reduction of Sinapic Acid and Sinapine in Rapeseed Meal.

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For the more efficient detoxification of phenolic compounds, a promising avenue would be to develop a multi-enzyme biocatalyst comprising peroxidase, laccase and other oxidases. However, the development of this multi-enzyme biocatalyst is limited by the vulnerability of fungal laccases and

CotA of Bacillus subtilis is a copper-dependent laccase.

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The spore coat protein CotA of Bacillus subtilis displays similarities with multicopper oxidases, including manganese oxidases and laccases. B. subtilis is able to oxidize manganese, but neither CotA nor other sporulation proteins are involved. We demonstrate that CotA is a laccase. Syringaldazine,

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