Back to Search
Start Over
NMR Study of the Exchange Coupling in the Trinuclear Cluster of the Multicopper Oxidase Fet3p.
- Source :
-
Journal of the American Chemical Society . 8/18/2010, Vol. 132 Issue 32, p11191-11196. 6p. 1 Diagram, 2 Graphs. - Publication Year :
- 2010
-
Abstract
- Fe2+ to Fe3+. 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 Cu2+ 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. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00027863
- Volume :
- 132
- Issue :
- 32
- Database :
- Academic Search Index
- Journal :
- Journal of the American Chemical Society
- Publication Type :
- Academic Journal
- Accession number :
- 53877198
- Full Text :
- https://doi.org/10.1021/ja1037148