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Unsaturated, Mixed‐Valence Diiron Dithiolate Model for the Hox State of the [FeFe] Hydrogenase

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Justice, Aaron K., Rauchfuss, Thomas B., Wilson, Scott R.·2007·Angewandte Chemie International Edition

Abstract

Chemists are closing in on functional and structural models for the [FeFe] hydrogenases. Oxidation of [Fe2(S2C2H4)(CO)3(PMe3)(dppv)] (dppv=cis-1,2-C2H2(PPh2)2) by one electron affords a mixed-valence model for the Hox state of the active site of the [FeFe] hydrogenases. Like the enzyme, this model exhibits the “rotated structure” and binds CO (see scheme). The radical character of the model is confirmed by its ready binding of NO.

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Metadata

Authors
Justice, A. K., Rauchfuss, T. B., & Wilson, S. R.
Venue
Angewandte Chemie International Edition
Publisher
Wiley
Published
2007-08-03
Volume
46
Issue
32
Pages
6152-6154
ISSN
  • 1433-7851 (ISSN-L)
  • 1521-3773
OpenAlex
W2036809572
Cited by
161
References
0
FWCI
12.52
Type
journal article
Language
en
Open access
green

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Justice, A. K., Rauchfuss, T. B., & Wilson, S. R. (2007). Unsaturated, Mixed‐Valence Diiron Dithiolate Model for the Hox State of the [FeFe] Hydrogenase. Angewandte Chemie International Edition. https://doi.org/10.1002/anie.200702224

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