Electron transfer (ET) reactions in proteins can involve metal and organic cofactors as well as amino acids. The redox-active aromatic amino acids, tryptophan and tyrosine, are particularly interesting because they have been shown to act as hopping sites for long-range ET chemistry. We discuss our recent efforts to study a biological ET reaction that involves a tryptophan radical in the protein azurin. Resonance Raman studies of isotopologues of tryptophan combined with measurements of ET and proton-transfer (PT) quantum yields help reveal the role of vibrations in ET and PT chemistry. These experiments also highlight the role of protein environment on biological redox chemistry.

Investigation of biological electron transfer via isotopologues and resonance Raman spectroscopy

2019 Spring National Meeting

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