Electronic structures of active sites in copper proteins: contributions to reactivity

Article Abstract:

The electronic structures of blue copper proteins, coupled binuclear copper proteins and multicopper oxidases were studied using spectroscopic techniques such as EPR, circular dichroism and extended X-ray absorption fine structure. The results showed that a d(sub x2-y2) ground state, which provided for long-range electron transfer, characterized blue copper proteins. Similarly, the spectroscopic analyses revealed the effects of trinuclear copper cluster sites on the oxygen reactivity of multicopper oxidases. Additionally, coupled binuclear copper proteins exhibited antiferromagnetism which failed to give EPR signals.

Metalloproteins, Electronic structure, Atomic structure, Electron paramagnetic resonance spectroscopy, Electron spectroscopy, Organometallic compounds

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Multicopper oxidases and oxygenases

Article Abstract:

Spectroscopic analysis of copper cluster enzymes shows that both the oxytyrosinase and the peroxy intermediates in laccase contain the O-O peroxide bond but have different geometric and electronic structures. The heme oxidases and oxygenases have a broken O-O bond. This enables Fe to achieve high oxidation states in the oxo species. Hemocyanin and tyrosinase have a coupled binuclear center and do not exhibit EPR signal due to strong anti-ferromagnetic coupling.

Observations, Spectrum analysis, Spectroscopy, Copper

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Geometric and electronic structure/function correlations of non-heme iron enzymes

Article Abstract:

Research designed to obtain geometric and electronic structural information about the reactions of a wide range of mononuclear non-heme iron enzymes is presented. It was possible to develop a general mechanistic strategy used by many of the non-heme ferrous enzymes.

Enzymes, Heme

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