Two-domain multicopper oxidases (2dMCOs) couple the four-electron reduction of dioxygen to the oxidation of a number of different substrates, including organic compounds and reduced ferricytochromes. The geometry of 2dMCO active sites is similar to that in other multicopper oxidases, but is formed by a significantly different protein architecture. This fold resembles the overall architecture of NO forming copper nitrite reductase (CuNIR). 2dMCOs are classified based on the location of their type-1 copper centers.
|Original language||English (US)|
|Title of host publication||Handbook of Metalloproteins|
|Subtitle of host publication||Volumes 4 & 5|
|Publisher||John Wiley and Sons Ltd.|
|Number of pages||9|
|ISBN (Print)||047071199X, 9780470711996|
|State||Published - 2010|