Sulfonated Diiron Complexes as Water-Soluble Models of the [FeFe]-Hydrogenase Enzyme Active Site
(2011) Inorganic Chemistry — Vol. 50, p. 5015-5026 (2011)
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- Abstract
- A series of diiron complexes developed as fundamental models of the two-iron subsite in the [FeFe]-hydrogenase enzyme active site show water-solubility by virtue of a sulfonate group incorporated into the SCH2NRCH2S- dithiolate unit that bridges two FeI(CO)2L moieties. The sulfanilic acid group imparts even greater water solubility in the presence of β-cyclodextrin, β-CyD, for which NMR studies suggest aryl-sulfonate inclusion into the cyclodextrin cavity as earlier demonstrated in the X-ray crystal structure of 1Na 3 2 β- CyD clathrate, where 1Na = Naþ(μ-SCH2N(C6H4SO3 )CH2S-)[Fe-(CO)3]2, (Singleton et al., J. Am. Chem. Soc. 2010, 132, 8870). Electrochemical analysis of the complexes for potential as electrocatalysts for proton reduction to H2 finds the presence of β-CyD to diminish response, possibly reflecting inhibition of structural rearrangements required of the diiron unit for a facile catalytic cycle. Advantages of the aryl sulfonate approach include entry into a variety of water-soluble derivatives from the well-known (μ-SRS)[Fe(CO)3]2 parent biomimetic, that are stable inO2-free aqueous solutions.
- Affiliations
Texas A&M University (USA) Department of Chemistry
Citations
Singleton, M., Crouthers, D. J., Duttweiler, R. P., Reibenspies, J. H., & Darensbourg, M. Y. (2011). Sulfonated Diiron Complexes as Water-Soluble Models of the [FeFe]-Hydrogenase Enzyme Active Site. Inorganic Chemistry, 50, 5015-5026. https://doi.org/10.1021/ic200272x (Original work published 2011)