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Reconstitution of [Fe]-hydrogenase using model complexes.

Seigo Shima1,2, Dafa Chen3, Tao Xu4

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Researchers reconstituted [Fe]-hydrogenase using cofactor mimics. A 2-hydroxy group on the mimic is crucial for hydrogenase activity, revealing a key step in hydrogen activation.

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Area of Science:

  • Biochemistry
  • Bioinorganic Chemistry
  • Enzyme Mechanisms

Background:

  • [Fe]-Hydrogenase catalyzes a vital step in methanogenesis, converting CO2 and H2.
  • The enzyme's active site features an iron-guanylylpyridinol cofactor with a unique ligand environment.
  • The precise mechanism of H2 activation by [Fe]-hydrogenase remains poorly understood.

Purpose of the Study:

  • To elucidate the mechanism of H2 activation by [Fe]-hydrogenase.
  • To investigate the role of the cofactor's ligand environment in enzyme activity.
  • To create semisynthetic enzymes using cofactor mimics for mechanistic studies.

Main Methods:

  • Reconstitution of [Fe]-hydrogenase from apoenzyme using two distinct FeGP cofactor mimics.
  • Characterization of semisynthetic enzymes' activity towards H2 binding and activation.
  • Density Functional Theory (DFT) computations to model reaction mechanisms.

Main Results:

  • Semisynthetic enzymes with FeGP cofactor mimics reproduced the active site's ligand environment.
  • Enzyme reconstituted with a 2-hydroxypyridine-containing mimic regained H2 activation activity.
  • Enzyme reconstituted with a 2-methoxypyridine mimic showed minimal activity.
  • DFT calculations supported a mechanism involving deprotonation of the 2-hydroxy group.

Conclusions:

  • The 2-hydroxy group of the 2-pyridinol ligand plays a critical role in [Fe]-hydrogenase activity.
  • The hydroxyl group acts as an internal base, facilitating heterolytic H2 cleavage.
  • This study provides mechanistic insights into H2 activation by [Fe]-hydrogenase.