Sandbox Reserved 1104
From Proteopedia
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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">Atsushi Shimizu, ''Myrothecium verrucaria'' Bilirubin Oxidase and Its Mutants for Potential Copper Ligands (1999)[https://doi.org/10.1021/bi9819531]</ref> | ||
== Function == | == Function == | ||
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== Applications == | == Applications == | ||
| - | 3. Biofuel cell | ||
| - | + | =====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.<ref name="bcell">A. de Poulpiquet, Reprinted from Electrochemistry Communications, Volume 42 (2014). [http://archives.cnrs.fr/inc/article/lojou]</ref> 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. <ref name="bcell2">A. de Poulpiquet, Design of a H2/O2 biofuel cell based on thermostable enzymes (2014). [https://doi.org/10.1016/j.elecom.2014.02.012]</ref> 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.<ref name="bcell"/> 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.<ref name="bcell2"/> | 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.<ref name="bcell">A. de Poulpiquet, Reprinted from Electrochemistry Communications, Volume 42 (2014). [http://archives.cnrs.fr/inc/article/lojou]</ref> 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. <ref name="bcell2">A. de Poulpiquet, Design of a H2/O2 biofuel cell based on thermostable enzymes (2014). [https://doi.org/10.1016/j.elecom.2014.02.012]</ref> 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.<ref name="bcell"/> 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.<ref name="bcell2"/> | ||
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References
- ↑ 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
- ↑ 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
- ↑ Wikipedia, Multicopper oxidase [1]
- ↑ Atsushi Shimizu, Myrothecium verrucaria Bilirubin Oxidase and Its Mutants for Potential Copper Ligands (1999)[2]
- ↑ 5.0 5.1 A. de Poulpiquet, Reprinted from Electrochemistry Communications, Volume 42 (2014). [3]
- ↑ 6.0 6.1 A. de Poulpiquet, Design of a H2/O2 biofuel cell based on thermostable enzymes (2014). [4]
