Synthetic support of de novo design: sterically bulky [FeFe]-hydrogenase models. Academic Article

abstract

• (Figure Presented) A twisted mimic: Upon oxidation of [(-SCH 2C(CH3)2CH2S-){Fe I(CO)2PMe3}2], rearrangement yields the mixed-valent FeIFeII cation in a square-pyramid/ inverted square-pyramid geometry with a semibridging CO ligand, closely mimicking the [FeFe] hydrogenase enzyme active site. According to de novo design principles, the steric effect of bridgehead bulk in the S-S bridging ligand stabilizes this structure in the absence of the protein matrix. 2008 Wiley-VCH Verlag GmbH & Co. KGaA.

authors

• Darensbourg, Marcetta

published proceedings

• Angew Chem Int Ed Engl

author list (cited authors)

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

citation count

• 138

complete list of authors

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

publication date

• November 2008

publisher

• Wiley  Publisher

published in

• Angewandte Chemie International Edition  Journal

keywords

• Catalytic Domain
• Crystallography, X-Ray
• Hydrogenase
• Models, Chemical
• Nuclear Magnetic Resonance, Biomolecular
• Protein Conformation

Digital Object Identifier (DOI)

• 10.1002/anie.200803939

start page

• 9492

end page

• 9495

volume

• 47

issue

• 49

URL

• http%3A%2F%2Fdx.doi.org%2F10.1002%2Fanie.200803939