Abstract
The Fe 4S 4 complex {(CH 3) 3NCH 2CONH 2} 2[Fe 4S 4(BuS) 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 (S y) of one tertbutylthiolate 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 [Fe 4S 4] 2+ cluster core. Additionally, this is the first synthetic Fd model in which N-H⋯S hydrogen bonding to a cluster has been achieved.
Original language | English (US) |
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Pages (from-to) | 3777-3779 |
Number of pages | 3 |
Journal | Inorganic Chemistry |
Volume | 44 |
Issue number | 11 |
DOIs | |
State | Published - May 30 2005 |
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ASJC Scopus subject areas
- Inorganic Chemistry
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N-H⋯S hydrogen bonds in a ferredoxin model. / Walters, Marc; Roche, Cara L.; Rheingold, Arnold L.; Kassel, Scott W.
In: Inorganic Chemistry, Vol. 44, No. 11, 30.05.2005, p. 3777-3779.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - N-H⋯S hydrogen bonds in a ferredoxin model
AU - Walters, Marc
AU - Roche, Cara L.
AU - Rheingold, Arnold L.
AU - Kassel, Scott W.
PY - 2005/5/30
Y1 - 2005/5/30
N2 - The Fe 4S 4 complex {(CH 3) 3NCH 2CONH 2} 2[Fe 4S 4(BuS) 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 (S y) of one tertbutylthiolate 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 [Fe 4S 4] 2+ cluster core. Additionally, this is the first synthetic Fd model in which N-H⋯S hydrogen bonding to a cluster has been achieved.
AB - The Fe 4S 4 complex {(CH 3) 3NCH 2CONH 2} 2[Fe 4S 4(BuS) 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 (S y) of one tertbutylthiolate 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 [Fe 4S 4] 2+ cluster core. Additionally, this is the first synthetic Fd model in which N-H⋯S hydrogen bonding to a cluster has been achieved.
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UR - http://www.scopus.com/inward/citedby.url?scp=20444438005&partnerID=8YFLogxK
U2 - 10.1021/ic048208z
DO - 10.1021/ic048208z
M3 - Article
C2 - 15907101
AN - SCOPUS:20444438005
VL - 44
SP - 3777
EP - 3779
JO - Inorganic Chemistry
JF - Inorganic Chemistry
SN - 0020-1669
IS - 11
ER -