A cyclodextrin host/guest approach to a hydrogenase active site biomimetic cavity. Academic Article

abstract

• The hydrophobic cavity of the active site of [FeFe]-Hydrogenase is mimicked by two cyclodextrin molecules which surround a 2Fe2S synthetic analogue of the active site, outfitted with an aryl sulfonate to promote inclusion into beta-cyclodextrin. The X-ray crystal structure of the clathrate shows an increased torsion angle between the apical CO ligands indicating that the supramolecular cage destabilizes the eclipsed geometry typical of diiron model complexes. Inclusion in the model second coordination sphere also has important effects on the electrochemical properties of the model complex including an approximately 80 mV shift of the Fe(I)Fe(I)/Fe(I)Fe(0) reduction and a change in the potential at which electrocatalytic reduction of protons by the diiron complex occurs.

authors

• Darensbourg, Marcetta

published proceedings

• J Am Chem Soc

author list (cited authors)

• Singleton, M. L., Reibenspies, J. H., & Darensbourg, M. Y.

citation count

• 126

complete list of authors

• Singleton, Michael L||Reibenspies, Joseph H||Darensbourg, Marcetta Y

publication date

• July 2010

publisher

• American Chemical Society (ACS)  Publisher

published in

• Journal of the American Chemical Society  Journal

keywords

• Biomimetics
• Catalytic Domain
• Crystallography, X-Ray
• Cyclodextrins
• Hydrogenase
• Iron-sulfur Proteins
• Models, Molecular

PubMed Central ID

• 20536241

Digital Object Identifier (DOI)

• 10.1021/ja103774j

start page

• 8870

end page

• 8871

volume

• 132

issue

• 26

URL

• http%3A%2F%2Fdx.doi.org%2F10.1021%2Fja103774j