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Spectroscopy in general is our cornerstone method. Transition metal complexes typically have color due to specific absorption of light. Changes in such absorption conveniently provide a sensitive probe for molecular events that occur in metalloenzymes. We exploit these probes to study what happens at individual reaction steps along enzymatic reaction cycle.
In our research we strive to extend common boundaries of traditional spectroscopic approaches, such as electronic and vibrational spectroscopies. We seek increase sensitivity of individual methods by combining complimentary spectroscopic methods with each other, with temporal or kinetic information, and with specific chemical and biological methods.
In the area of electronic absorption spectroscopy we are exploring far UV region. Our current goal is to characterize spectral signatures of common redox-active metal cofactors as well as several amino acid residues and their radicals forms in the region between 200 and 300 nm.
In the domain of vibrational spectroscopy we analyze changes in motion of individual atoms or their groups along the reaction path using infrared absorption or resonance Raman methods. By using stable isotope substitution of molecular oxygen, water, metal, or substrate we can make specific vibrational assignments, thus revealing subtle structural changes from one species to another.
We are developing cryogenic continuous flow method that allows to create a pseudo-steady state conditions at temperatures as low as -70oC. In combination with resonance Raman spectroscopy this method allows to study directly transient events in enzymatic systems at atomic resolution. .
We combine spectroscopic analysis with variety methods from across several chemical disciplines:
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