Abstract
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 |
| Editors | Albrecht Messerschmidt |
| Publisher | John Wiley and Sons Ltd. |
| Pages | 591-599 |
| Number of pages | 9 |
| ISBN (Print) | 047071199X, 9780470711996 |
| State | Published - 2010 |