The organometallic active site of [Fe]hydrogenase: Models and entatic states
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Edited by Jack Halpern, University of Chicago, Chicago, IL, and approved January 13, 2003 (received for review November 14, 2002)
Abstract
The simple organometallic, (μ-S2)Fe2(CO)6, serves as a precursor to synthetic analogues of the chemically rudimentary iron-only hydrogenase enzyme active site. The fundamental properties of the (μ-SCH2CH2CH2S)[Fe(CO)3]2 compound, including structural mobility and regioselectivity in cyanide/carbon monoxide substitution reactions, relate to the enzyme active site in the form of transition-state structures along reaction paths rather than ground-state structures. Even in the absence of protein-based active-site organization, the ground-state structural model complexes are shown to serve as hydrogenase enzyme reaction models, H2 uptake and H2 production, with the input of photo- or electrochemical energy, respectively.
Footnotes
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↵ * To whom correspondence should be addressed. E-mail: marcetta{at}mail.chem.tamu.edu.
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This paper was submitted directly (Track II) to the PNAS office.
- Abbreviation:
- H2ase,
- hydrogenase
- Copyright © 2003, The National Academy of Sciences
