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ENDOR Characterization of (N

Hao Yang1, Jonathan Rittle2, Amy R Marts1

  • 1Department of Chemistry , Northwestern University , Evanston , Illinois 60208 , United States.

Inorganic Chemistry
|September 18, 2018
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Summary
This summary is machine-generated.

A biomimetic diiron complex models nitrogenase enzyme states, revealing insights into nitrogen (N2) reduction. This study confirms a delocalized mixed valency and uses hydride properties as a diagnostic signature for biological iron-sulfur clusters.

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Area of Science:

  • Bioinorganic Chemistry
  • Enzyme Mechanisms
  • Organometallic Chemistry

Background:

  • Nitrogenase is a crucial enzyme that reduces atmospheric nitrogen (N2) to ammonia.
  • Understanding nitrogenase mechanisms requires biomimetic models that replicate its active site.
  • The enzyme's catalytic cycle involves complex iron-sulfur clusters and hydride intermediates.

Purpose of the Study:

  • To model key intermediates in the nitrogenase catalytic cycle using a biomimetic diiron complex.
  • To investigate the electronic structure and bonding of a diiron complex with bound N2 and bridging hydrides.
  • To establish diagnostic signatures for identifying similar structures in biological systems.

Main Methods:

  • Synthesis of a biomimetic diiron complex, 4-(N2)2.
  • 1H and 14N 35 GHz ENDOR spectroscopy.
  • Analysis using a point-dipole model for dipolar interactions.

Main Results:

  • The diiron complex exhibits a Robin-Day type-III mixed valency, indicating delocalized electrons.
  • Bridging hydrides show a rhombic dipolar tensor, serving as a diagnostic signature for biological iron centers.
  • Spectroscopic analysis provides insights into charge transfer between iron and coordinated nitrogen.

Conclusions:

  • The biomimetic complex accurately models key states of nitrogenase, including the Janus intermediate.
  • The rhombic hydride signature is a valuable tool for studying nitrogenase and related metalloenzymes.
  • This work advances the understanding of N2 activation and reduction mechanisms in biological systems.