Electron transfer systems that drive photosynthetic respiration involve metalloproteins. Type 1 blue copper proteins are an important group of metalloproteins with redox potentials ranging from +372 mV to +680 mV.1,2 The large redox potentials offer insight into the unusually stable CuI center.2 Organic macrocycles have been designed to increase the redox potentials with copper and are of current interest within our group. Cryptands L2 and L3 have been synthesized from 14[ane]N2S2 (L1) in adequate yields. The cavity within the cryptand core encapsulates select metals and L3 has been shown to stabilize CuI from the initial CuII oxidation state. Research has been focused on CuII/CuI potentials and the rate at which the oxidation states interconvert with L3. Use of X-ray Crystallography, Electron Paramagnetic Resonance (EPR), and Ultra-violet/Visible Spectroscopy will be crucial for the determination of copper potentials and binding modes. This presentation will emphasize the synthetic challenge of L2, L3, and metal-ligand binding. References a) Tolman, W. B.; Yang, L. J. Biol. Inorg. Chem. 2012, 17, 285-291 b) Gray, H. B.; Malmstrom, B. G.; Williams, R. J. P. J. Biol. Inorg. Chem. 2000, 5, 551-559. Sanderson, D. G.; Anderson, L. B.; Gross, E. L. Biochim. Biophys. Acta. 1986, 3, 269-78

Stabilized copper(I) N,S containing cryptands

249th National Meeting (2015)

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