Sandbox Reserved 1104

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Multicopper oxidases are enzymes which oxidise their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre.<ref>Wikipedia, Multicopper oxidase [https://en.wikipedia.org/wiki/Multicopper_oxidase]</ref>
Multicopper oxidases are enzymes which oxidise their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre.<ref>Wikipedia, Multicopper oxidase [https://en.wikipedia.org/wiki/Multicopper_oxidase]</ref>
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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.<ref name="multic">DOI 10.1021/bi9819531</ref>
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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.<ref name="multic">DOI 10.1021/bi9819531</ref>
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.<ref name="multic"/>
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.<ref name="multic"/>

Revision as of 13:54, 12 January 2020

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.
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References

  1. Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
  3. [1]). The 2xII form is a 4 chain structure with 8 ligands NAG-NAG belonging to the family of oxidoreductases. It was first isolated in 1981 by the scientists Sawao Murao and Noriaki Tanaka as they tried to find a microorganism able to decolore raw sewage and to use it as an analytical tool in clinical fields. Now, bilirubin oxidase may be used to determine free hemoglobin in icteric specimens and can be use as a treatment for neonatal jaundice. Moreover, the bilirubin oxidase is an enzyme that is active in porphyrin and chlorophyll metabolism.

    Structure

    Multicopper oxidases are enzymes which oxidise their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre.<ref>Wikipedia, Multicopper oxidase [https://en.wikipedia.org/wiki/Multicopper_oxidase]</li> <li id="cite_note-multic-3">↑ <sup>[[#cite_ref-multic_3-0|4.0]]</sup> <sup>[[#cite_ref-multic_3-1|4.1]]</sup> <sup>[[#cite_ref-multic_3-2|4.2]]</sup> Shimizu A, Kwon JH, Sasaki T, Satoh T, Sakurai N, Sakurai T, Yamaguchi S, Samejima T. Myrothecium verrucaria bilirubin oxidase and its mutants for potential copper ligands. Biochemistry. 1999 Mar 9;38(10):3034-42. doi: 10.1021/bi9819531. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10074356 10074356] doi:[http://dx.doi.org/10.1021/bi9819531 http://dx.doi.org/10.1021/bi9819531]</li> <li id="cite_note-bcell-4">↑ <sup>[[#cite_ref-bcell_4-0|5.0]]</sup> <sup>[[#cite_ref-bcell_4-1|5.1]]</sup> A. de Poulpiquet, A. Ciaccafava, R. Gadiou, S. Gounel, M.T. Giudici-Orticoni, N. Mano, E. Lojou, Reprinted from Electrochemistry Communications, Volume 42 (2014). [http://archives.cnrs.fr/inc/article/lojou]</li> <li id="cite_note-bcell2-5">↑ <sup>[[#cite_ref-bcell2_5-0|6.0]]</sup> <sup>[[#cite_ref-bcell2_5-1|6.1]]</sup> A. de Poulpiquet, A. Ciaccafava, R. Gadiou, S. Gounel, M.T. Giudici-Orticoni, N. Mano, E. Lojou, Design of a H2/O2 biofuel cell based on thermostable enzymes (2014) [ https://doi.org/10.1016/j.elecom.2014.02.012

    ]</li></ol></ref>
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