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A Genetically Encoded Two-Dimensional Infrared Probe for Enzyme Active-Site Dynamics.

Li Wang1,2, Jia Zhang3,4, Ming-Jie Han5,6

  • 1School of Life Sciences, University of Chinese Academy of Sciences, Yuquan Road, Shijingshan District, Beijing, 100049, China.

Angewandte Chemie (International Ed. in English)
|March 1, 2021
PubMed
Summary

Researchers developed a new probe to study enzyme active-site water dynamics using two-dimensional infrared (2D-IR) spectroscopy. This method reveals how enzyme motions influence chemical reactions.

Keywords:
azido-tyrosineinfrared spectroscopymetalloenzymesunnatural amino acidwater

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Area of Science:

  • Biophysical Chemistry
  • Enzyme Kinetics
  • Spectroscopy

Background:

  • Two-dimensional infrared (2D-IR) spectroscopy tracks ultrafast water dynamics around proteins.
  • Probing enzyme active-site dynamics is challenging due to a lack of specific probes.

Purpose of the Study:

  • To genetically incorporate a novel 2D-IR probe, m-azido-L-tyrosine (N3Y), into an enzyme active site.
  • To investigate enzyme active-site water motion and its relation to enzyme activity.

Main Methods:

  • Genetic incorporation of N3Y into the DddK enzyme.
  • Utilizing 2D-IR spectroscopy to monitor active-site water dynamics.
  • Assessing enzyme activity under varying conditions (iron oxidation, denaturation).

Main Results:

  • N3Y was successfully incorporated into the DddK active site.
  • Active-site water motion was confined.
  • Enzyme activity decreased with iron oxidation and denaturation, correlating with water motion changes.

Conclusions:

  • The N3Y probe enables site-specific 2D-IR studies of enzyme active sites.
  • Femtosecond-picosecond active-site motions are crucial for enzyme function.
  • N3Y is a broadly applicable tool for studying enzyme mechanisms.