Sandbox Reserved 1104

This Sandbox is Reserved from 25/11/2019, through 30/9/2020 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1091 through Sandbox Reserved 1115.

To get started: Click the edit this page tab at the top. Save the page after each step, then edit it again. show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page. Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc. More help: Help:Editing

Your Heading Here (maybe something like 'Structure')

spinqualitylabelsall models Caption for this structure Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D This is a default text for your page '. Click above on edit this page' to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia or to the article describing Jmol to the rescue. Introduction Bilirubin oxidase is an enzyme known to catalyze the oxidation of bilirubin to biliverdin by reducting O2 in water. It’s a multicopper oxidase which can exist under two different structures in the ascomycete Myrothecium verrucaria (see the 3abg one Bilirubin oxidases are multicopper oxidases containing type 1, type 2, and type 3 coppers. Indeed, there is strong sequence homology between bilirubin oxidase and multicopper oxidases like laccase, ascorbate oxidase and even ceruloplasmin. Moreover, the His-Cys-His sequence, characteristic of multicopper oxidase, is present in bilirubin oxidase. Copper is essential for the enzyme activity. Copper is classified into three types according to their optical and magnetic properties. Type 1 copper (or blue copper) shows many charge-transfer bands around 450 nm, 600 nm and 750 nm. The most peculiar band appears around 600 nm and represents the Cys to Cu(II) charge transfer. Type 2 copper (or nonblue copper) does not show any strong charge-transfer bands in the visible region. Type 3 coppers are not detectable by ESR because some are antiferromagnetically coupled. However, a hydroxide ion links them and so gives a strong absorption at 330 nm. While type 2 and 3 coppers reduce dioxygen to two water molecules by forming a trinuclear center, type 1 copper transfers electrons from substrate to the trinuclear center. This is the peculiar sequence His456-Cys457-His458 that forms an intramolecular electron-transfer pathway between the type 1 copper site and the trinuclear center composed of the type 2 and type 3 copper sites. Applications 3. Biofuel cell In the field of power generation, biofuel cells provide an alternative to fossil energy. So far biofuell cells that were developed required specific enzymes that degrade and transform substrates present in physiologic fluids such as glucose and O2. These biofuel cells were used for medical devices power supply. Now a new generation of biofuel cells use hydrogenase. Indeed, H2/O2 biofuel cells are designed based on two thermostable enzymes: an hyperthermophilic O2-tolerant hydrogenase for H2 oxidation and bilirubin oxidase for O2 reduction. Both enzymes are immobilized on carbon nanofibers. This biofuel cell can deliver electricity over a wide range of températures and pH. Indeed, the thermostability of the enzymes allows the biofuel cell to work under extreme conditions, from 30 to 80°C. H2/O2 biofuel cells can be used as alternative power supply for small electronic devices in a sustainable manner. However, research is ongoing; one issue is the enzyme instability on long term. This is a sample scene created with SAT to color by Group, and another to make a transparent representation of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.