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Crystallographic and FTIR Spectroscopic Evidence of Changes in Fe Coordination Upon Reduction of the Active Site of the Fe-Only Hydrogenase from Desulfovibriodesulfuricans

Nicolet, Yvain, de Lacey, Antonio L., Vernède, Xavier, Fernandez, Victor M., Hatchikian, E. Claude, Fontecilla-Camps, Juan C.·2001·Journal of the American Chemical Society
DOI 10.1021/ja0020963
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Abstract

Fe-only hydrogenases, as well as their NiFe counterparts, display unusual intrinsic high-frequency IR bands that have been assigned to CO and CN(-) ligation to iron in their active sites. FTIR experiments performed on the Fe-only hydrogenase from Desulfovibrio desulfuricans indicate that upon reduction of the active oxidized form, there is a major shift of one of these bands that is provoked, most likely, by the change of a CO ligand from a bridging position to a terminal one. Indeed, the crystal structure of the reduced active site of this enzyme shows that the previously bridging CO is now terminally bound to the iron ion that most likely corresponds to the primary hydrogen binding site (Fe2). The CO binding change may result from changes in the coordination sphere of Fe2 or its reduction. Superposition of this reduced active site with the equivalent region of a NiFe hydrogenase shows a remarkable coincidence between the coordination of Fe2 and that of the Fe ion in the NiFe cluster. Both stereochemical and mechanistic considerations suggest that the small organic molecule found at the Fe-only hydrogenase active site and previously modeled as 1,3-propanedithiolate may, in fact, be di-(thiomethyl)-amine.

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Metadata

Authors
Nicolet, Y., de Lacey, A. L., Vernède, X., Fernandez, V. M., Hatchikian, E. C., & Fontecilla-Camps, J. C.
Venue
Journal of the American Chemical Society
Publisher
American Chemical Society (ACS)
Published
2001-02-01
Volume
123
Issue
8
Pages
1596-1601
ISSN
  • 0002-7863 (ISSN-L)
  • 1520-5126
DOI
10.1021/ja0020963
OpenAlex
W2062220773
Cited by
786
References
1
FWCI
26.85
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Crystallographic and FTIR Spectroscopic Evidence of Changes in Fe Coordination Upon Reduction of the Active Site of the Fe-Only Hydrogenase from Desulfovibriodesulfuricans. https://app.cochat.ai/papers/10.1021/ja0020963
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Nicolet, Y., de Lacey, A. L., Vernède, X., Fernandez, V. M., Hatchikian, E. C., & Fontecilla-Camps, J. C. (2001). Crystallographic and FTIR Spectroscopic Evidence of Changes in Fe Coordination Upon Reduction of the Active Site of the Fe-Only Hydrogenase from Desulfovibriodesulfuricans. Journal of the American Chemical Society. https://doi.org/10.1021/ja0020963

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