NMR Study of the Exchange Coupling in the Trinuclear Cluster of the Multicopper Oxidase Fet3p
Citations Over TimeTop 18% of 2010 papers
Abstract
Fet3p from Saccharomyces cerevisiae is a multicopper oxidase (MCO) which oxidizes Fe(2+) to Fe(3+). The electronic structure of the different copper centers in this family of enzymes has been extensively studied and discussed for years with a particular focus on the exchange coupling regime in the trinuclear cluster (TNC). Using NMR spectroscopy we have quantified the exchange coupling constant in the type 3 center in a fully metalated oxidase; this value in Fet3p is significantly higher than that reported for proteins containing isolated type 3 centers as tyrosinase. We also provide evidence of exchange coupling between the type 2 and the type 3 Cu(2+) ions, which supports the crystallographic evidence of dioxygen binding to the TNC. This work provides the foundation for the application of NMR to these complex systems.
Related Papers
- → Structural insights into the O2reduction mechanism of multicopper oxidase(2015)77 cited
- → The Involvement of a Multicopper Oxidase in Iron Uptake by the Green Algae Chlamydomonas reinhardtii(2002)108 cited
- → Three-dimensional organization of three-domain copper oxidases: A review(2008)58 cited
- → The multicopper oxidase CutO confers copper tolerance toRhodobacter capsulatus(2006)32 cited