Two-Domain Multicopper Oxidase

T. J. Lawton, Amy C Rosenzweig

Research output: Chapter in Book/Report/Conference proceedingChapter

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 languageEnglish (US)
Title of host publicationHandbook of Metalloproteins
Subtitle of host publicationVolumes 4 & 5
EditorsAlbrecht Messerschmidt
PublisherJohn Wiley and Sons Ltd.
Pages591-599
Number of pages9
ISBN (Print)047071199X, 9780470711996
StatePublished - 2010

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    Lawton, T. J., & Rosenzweig, A. C. (2010). Two-Domain Multicopper Oxidase. In A. Messerschmidt (Ed.), Handbook of Metalloproteins: Volumes 4 & 5 (pp. 591-599). John Wiley and Sons Ltd..