NMR study of the exchange coupling in the trinuclear cluster of the multicopper oxidase fet3p.
Related Articles NMR study of the exchange coupling in the trinuclear cluster of the multicopper oxidase fet3p.
J Am Chem Soc. 2010 Aug 18;132(32):11191-6
Authors: Zaballa ME, Ziegler L, Kosman DJ, Vila AJ
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.
PMID: 20698686 [PubMed - in process]
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PubMed