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CotA
    RR spectroscopy is a powerful tool for investigating the coordination geometry of the Cu2+ in the T1 site of multicopper oxygen reductases. By using the charge transfer excitation, an estimation of the Cu-S(Cys) bond length can be extracted from the RR spectra, which has a direct correlation with standard enthalpy of Cu2+ reduction, redox potential of T1 site and other thermodynamic parameters in laccases.
    We use RR spectroscopy in order to understand the role of the Cu-S bond strength in controlling the spectroscopic, electrochemical and catalytic features of the T1 copper site of CotA and specially designed mutants with tuned electrochemical features, which possess potentially interesting and diverse biotechnological applications.


     Spectroscopy
     Raman
     Resonance Raman
     Surface Enhanced
     Resonance 
Raman
     Time Resolved SERR    
     Proteins
     Heme
     Blue copper
     Non hemic iron
     Iron sulfur
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