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Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors
Published on: September 13, 2013
Model studies of azide binding to functional analogues of CcO
James P Collman1, Abhishek Dey, Richard A Decréau
1Department of Chemistry, Stanford University, Stanford, CA 94305, USA. jpc@stanford.edu
Abstract:
N3- binding to a functional model of CcO is investigated in its Fe3+, Fe3+Cu+, and Fe3+Cu2+ forms. A combination of EPR and FTIR indicates that N3- binds in a bridging mode in the bimetallic sites and signature N3- bands are identified for several forms of N3- binding to the site. The presence of the distal metal increases the binding affinity of N3-. This bridging enables antiferromagnetic interaction between the two metal centers in the Fe3+Cu2+ state, which results in an EPR-silent ground state.
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