Development of Time-resolved X-ray Crystallographic and Spectroscopic Methodologies for Metalloenzymes Restricted; Files & ToC

Emamian, Sahand (Fall 2021)

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The emergence of high-intensity X-ray synchrotron sources has opened the door to uncovering the electronic and atomic structure of macromolecules, such as metalloenzymes. These biological catalysts use metal ions to perform otherwise unfavorable biochemical reactions. Knowledge of their structure and function not only has the potential to inspire innovations in the fields of health and energy, but can also help us understand the fundamental physics of biological processes. X-ray methods, such as X-ray emission spectroscopy and X-ray crystallography, are powerful tools capable of elucidating electronic and atomic structure, respectively. Moreover, pump-probe techniques allow time-resolution of metalloenzyme reactions. Toward the eventual goal of tandem, time-resolved X-ray crystallography and spectroscopy at the Advanced Photon Source of Argonne National Lab, we have developed a sample delivery method, and significant progress has been made toward anaerobic mounting of protein crystals. We have also developed and tested an iron Kβ emission spectrometer, which yielded promising results on an iron-dependent metalloenzyme crystal. 

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