TY - JOUR
T1 - Photoelectron spectroscopy of dithiolatodiironhexacarbonyl models for the active site of [Fe-Fe] hydrogenases
T2 - Insight into the reorganization energy of the "rotated" structure in the enzyme
AU - Petro, Benjamin J.
AU - Vannucci, Aaron K.
AU - Lockett, L. Tori
AU - Mebi, Charles
AU - Kottani, Rudresha
AU - Gruhn, Nadine E.
AU - Nichol, Gary S.
AU - Goodyer, Paul A.J.
AU - Evans, Dennis H.
AU - Glass, Richard S.
AU - Lichtenberger, Dennis L.
N1 - Funding Information:
The authors thank Dr. Allen G. Oliver, University of California, Santa Cruz, for data collection of 6 . The support of the National Science Foundation through the Collaborative Research in Chemistry program, Grant No. CHE 0527003, is gratefully acknowledged.
PY - 2008/11/12
Y1 - 2008/11/12
N2 - Synthetic analogs, μ-(RS)2Fe2(CO)6, of the active site of [Fe-Fe] hydrogenases do not have the semi-bridged CO and "rotated" structure found in the enzyme. However, recent studies have shown that cations of dithiolatodiiron complexes adopt this rotated structure. This paper reports the use of photoelectron spectroscopy in combination with density functional theory calculations to show that two previously reported complexes: μ-(1,2-benzenedithiolato)Fe2(CO)6 and μ-(1,3-propanedithiolato)Fe2(CO)6 and two new complexes: μ-(2,3-pyridinodithiolato)Fe2(CO)6 and μ-(norbornane-2-exo,3-exo-dithiolato)Fe2(CO)6 favor the "rotated" structure in their corresponding cations. Furthermore, these methods provide a measure of the reorganization energy between the "rotated" and "unrotated" structures in the gas phase. The results provide insight on the entatic state of the dithiolatodiiron site in the enzyme, in which the protein controls the structure of the active site. This structure influences the redox energy and reorganization energy enabling fast electron transfer.
AB - Synthetic analogs, μ-(RS)2Fe2(CO)6, of the active site of [Fe-Fe] hydrogenases do not have the semi-bridged CO and "rotated" structure found in the enzyme. However, recent studies have shown that cations of dithiolatodiiron complexes adopt this rotated structure. This paper reports the use of photoelectron spectroscopy in combination with density functional theory calculations to show that two previously reported complexes: μ-(1,2-benzenedithiolato)Fe2(CO)6 and μ-(1,3-propanedithiolato)Fe2(CO)6 and two new complexes: μ-(2,3-pyridinodithiolato)Fe2(CO)6 and μ-(norbornane-2-exo,3-exo-dithiolato)Fe2(CO)6 favor the "rotated" structure in their corresponding cations. Furthermore, these methods provide a measure of the reorganization energy between the "rotated" and "unrotated" structures in the gas phase. The results provide insight on the entatic state of the dithiolatodiiron site in the enzyme, in which the protein controls the structure of the active site. This structure influences the redox energy and reorganization energy enabling fast electron transfer.
KW - Density functional theory
KW - Hydrogenase
KW - Metal-carbonyl clusters
KW - Photoelectron spectroscopy
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U2 - 10.1016/j.molstruc.2008.04.024
DO - 10.1016/j.molstruc.2008.04.024
M3 - Article
AN - SCOPUS:53849113640
VL - 890
SP - 281
EP - 288
JO - Journal of Molecular Structure
JF - Journal of Molecular Structure
SN - 0022-2860
IS - 1-3
ER -