N-H...S hydrogen bonds in a ferredoxin model.
The Fe4S4 complex {(CH3)3NCH2CONH2}2[Fe4S4((tBuS)4] (1) was synthesized to replicate the ferredoxin active site with a subset of its N-H...S hydrogen bonds. The two cationic counterions mimic the polypeptide backbone of ferredoxin (Fd) as amide hydrogen-bond donors to sulfur atoms of the iron-sulfur cluster. X-ray crystallographic data show that the organic sulfur (Sgamma) of one tert-butylthiolate ligand and one inorganic sulfur of the cluster core serve as N-H...S hydrogen-bond acceptors. The cluster core of complex 1 is tetragonally elongated in contrast to that of Fd, which is tetragonally compressed. This is the first observation of an elongated [Fe4S4]2+ cluster core. Additionally, this is the first synthetic Fd model in which N-H...S hydrogen bonding to a cluster has been achieved.
Walters
Marc A
MA
Department of Chemistry, New York University, New York, New York 10003, USA. marc.walters@nyu.edu
Roche
Cara L
CL
Rheingold
Arnold L
AL
Kassel
Scott W
SW
D001665:Binding Sites; D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D007501:Iron / Q000737:chemistry; D007506:Iron-Sulfur Proteins / Q000138:chemical synthesis* / Q000737:chemistry*; D008958:Models, Molecular; D008968:Molecular Conformation; D013455:Sulfur / Q000737:chemistry
C501376:(CH3)3NCH2CONH2)2(Fe4S4((tBuS)4); D007506:Iron-Sulfur Proteins; D013455:Sulfur; D007501:Iron