Molecular and biochemical characterization of a highly stable bacterial laccase that occurs as a structural component of the Bacillus subtilis endospore coat.
24 May 2002-Journal of Biological Chemistry (American Society for Biochemistry and Molecular Biology)-Vol. 277, Iss: 21, pp 18849-18859
TL;DR: This model of CotA contains all the structural features of a laccase, including the reactive surface-exposed copper center (T1) and two buried copper centers (T2 and T3), and shows a half-life of inactivation at 80 °C of about 4 and 2 h, indicating that CotA is intrinsically highly thermostable.
About: This article is published in Journal of Biological Chemistry.The article was published on 2002-05-24 and is currently open access. It has received 502 citations till now. The article focuses on the topics: Endospore coat & Multicopper oxidase.
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TL;DR: The fact that laccases only require molecular oxygen for catalysis makes them suitable for biotechnological applications for the transformation or immobilization of xenobiotic compounds.
Abstract: Laccases of fungi attract considerable attention due to their possible involvement in the transformation of a wide variety of phenolic compounds including the polymeric lignin and humic substances. So far, more than a 100 enzymes have been purified from fungal cultures and characterized in terms of their biochemical and catalytic properties. Most ligninolytic fungal species produce constitutively at least one laccase isoenzyme and laccases are also dominant among ligninolytic enzymes in the soil environment. The fact that they only require molecular oxygen for catalysis makes them suitable for biotechnological applications for the transformation or immobilization of xenobiotic compounds.
1,925 citations
TL;DR: Escherichia coli is equipped with multiple systems to ensure safe copper handling under varying environmental conditions, but pathways of copper uptake and intracellular copper handling are still not identified in E. coli.
Abstract: Escherichia coli is equipped with multiple systems to ensure safe copper handling under varying environmental conditions. The Cu(I)-translocating P-type ATPase CopA, the central component in copper homeostasis, is responsible for removing excess Cu(I) from the cytoplasm. The multi-copper oxidase CueO and the multi-component copper transport system CusCFBA appear to safeguard the periplasmic space from copper-induced toxicity. Some strains of E. coli can survive in copper-rich environments that would normally overwhelm the chromosomally encoded copper homeostatic systems. Such strains possess additional plasmid-encoded genes that confer copper resistance. The pco determinant encodes genes that detoxify copper in the periplasm, although the mechanism is still unknown. Genes involved in copper homeostasis are regulated by MerR-like activators responsive to cytoplasmic Cu(I) or two-component systems sensing periplasmic Cu(I). Pathways of copper uptake and intracellular copper handling are still not identified in E. coli.
675 citations
TL;DR: This review summarises the methodologies used to evaluate the toxicity of azo dyes and their degradation products and discusses the recent studies on the decolouration or degradation using algae, yeast, filamentous fungi and bacteria, genetically modified microorganisms and microbiological systems combined with Advanced Oxidation Processes and Microbial Fuel Cells.
672 citations
TL;DR: There is strong evidence for their widespread distribution in prokaryotes and the first crystal structure of a bacterial laccase is already available, indicating their high non-specific oxidation capacity.
629 citations
TL;DR: It is shown that long-range electron transfer between these enzymes and electrodes can be established, and the mechanistic schemes of the DET processes are proposed.
557 citations
Cites background from "Molecular and biochemical character..."
...…of curren erest include screening of Lc sources, studying new lac Shin and Lee, 2000; Xu et al., 2000; Koroleva et al., 20 lonowska et al., 2002; Martins et al., 2002; Palmer et 003), investigating the structure of the enzyme (Antorini et l., 2001; Hakulinen et al., 2002; Piontek et al., 2002;…...
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TL;DR: This assay is very reproducible and rapid with the dye binding process virtually complete in approximately 2 min with good color stability for 1 hr with little or no interference from cations such as sodium or potassium nor from carbohydrates such as sucrose.
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TL;DR: The PROCHECK suite of programs as mentioned in this paper provides a detailed check on the stereochemistry of a protein structure and provides an assessment of the overall quality of the structure as compared with well refined structures of the same resolution.
Abstract: The PROCHECK suite of programs provides a detailed check on the stereochemistry of a protein structure Its outputs comprise a number of plots in PostScript format and a comprehensive residue-by-residue listing These give an assessment of the overall quality of the structure as compared with well refined structures of the same resolution and also highlight regions that may need further investigation The PROCHECK programs are useful for assessing the quality not only of protein structures in the process of being solved but also of existing structures and of those being modelled on known structures
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TL;DR: The MOLSCRIPT program as discussed by the authors produces plots of protein structures using several different kinds of representations, including simple wire models, ball-and-stick models, CPK models and text labels.
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TL;DR: A comparative protein modelling method designed to find the most probable structure for a sequence given its alignment with related structures, which is automated and illustrated by the modelling of trypsin from two other serine proteinases.
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TL;DR: Raster3D is discussed, which is a suite of programs for molecular graphics, which must compromise the quality of rendered images to achieve rendering speeds high enough for useful interactive manipulation of three-dimensional objects.
Abstract: Publisher Summary This chapter discusses Raster3D, which is a suite of programs for molecular graphics. Crystallographers were among the first and most avid consumers of graphics workstations. Rapid advances in computer hardware, and particularly in the power of specialized computer graphics boards, have led to successive generations of personal workstations with ever more impressive capabilities for interactive molecular graphics. For many years, it was standard practice in crystallography laboratories to prepare figures by photographing directly from the workstation screen. No matter how beautiful the image on the screen, however, this approach suffers from several intrinsic limitations. Among these is the inherent limitation imposed by the effective resolution of the screen. Use of the graphics hardware in a workstation to generate images for later presentation can also impose other limitations. Designers of workstation hardware must compromise the quality of rendered images to achieve rendering speeds high enough for useful interactive manipulation of three-dimensional objects.
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