3qpk
From Proteopedia
(Difference between revisions)
| Line 10: | Line 10: | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/LAC1_MELAO LAC1_MELAO] Lignin degradation and detoxification of lignin-derived products (Probable).<ref>PMID:15474046</ref> | [https://www.uniprot.org/uniprot/LAC1_MELAO LAC1_MELAO] Lignin degradation and detoxification of lignin-derived products (Probable).<ref>PMID:15474046</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Laccases catalyze the oxidation of phenolic substrates and the concominant reduction of dioxygen to water. We used xenon as an oxygen probe in search of routes for the entry of dioxygen into the catalytic center. Two xenon-pressurized crystal structures of recombinant Melanocarpus albomyces laccase were determined, showing three hydrophobic Xe-binding sites located in domain C. The analysis of hydrophobic cavities in other laccase structures further suggested the preference of domain C for binding of hydrophobic species such as dioxygen, thus suggesting that the hydrophobic core of domain C could function as a channel through which dioxygen can enter the trinuclear copper center. | ||
| + | |||
| + | Probing the Dioxygen Route in Melanocarpus albomyces Laccase with Pressurized Xenon Gas.,Kallio JP, Rouvinen J, Kruus K, Hakulinen N Biochemistry. 2011 May 5. PMID:21524088<ref>PMID:21524088</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3qpk" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
Current revision
Probing oxygen channels in Melanocarpus albomyces laccase
| |||||||||||
