Photoelectron spectroscopy of dithiolatodiironhexacarbonyl models for the active site of [Fe-Fe] hydrogenases: Insight into the reorganization energy of the "rotated" structure in the enzyme

Benjamin J. Petro; Aaron K. Vannucci; L. Tori Lockett; Charles Mebi; Rudresha Kottani; Nadine E. Gruhn; Gary S. Nichol; Paul A.J. Goodyer; Dennis H. Evans; Richard S. Glass; Dennis L. Lichtenberger

doi:10.1016/j.molstruc.2008.04.024

Photoelectron spectroscopy of dithiolatodiironhexacarbonyl models for the active site of [Fe-Fe] hydrogenases: Insight into the reorganization energy of the "rotated" structure in the enzyme

Benjamin J. Petro, Aaron K. Vannucci, L. Tori Lockett, Charles Mebi, Rudresha Kottani, Nadine E. Gruhn, Gary S. Nichol, Paul A.J. Goodyer, Dennis H. Evans, Richard S. Glass, Dennis L. Lichtenberger

Chemistry and Biochemistry

Research output: Contribution to journal › Article › peer-review

31 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	281-288
Number of pages	8
Journal	Journal of Molecular Structure
Volume	890
Issue number	1-3
DOIs	https://doi.org/10.1016/j.molstruc.2008.04.024
State	Published - Nov 12 2008

Keywords

Density functional theory
Hydrogenase
Metal-carbonyl clusters
Photoelectron spectroscopy

ASJC Scopus subject areas

Analytical Chemistry
Spectroscopy
Organic Chemistry
Inorganic Chemistry

Access to Document

10.1016/j.molstruc.2008.04.024

Cite this

Petro, B. J., Vannucci, A. K., Lockett, L. T., Mebi, C., Kottani, R., Gruhn, N. E., Nichol, G. S., Goodyer, P. A. J., Evans, D. H., Glass, R. S., & Lichtenberger, D. L. (2008). Photoelectron spectroscopy of dithiolatodiironhexacarbonyl models for the active site of [Fe-Fe] hydrogenases: Insight into the reorganization energy of the "rotated" structure in the enzyme. Journal of Molecular Structure, 890(1-3), 281-288. https://doi.org/10.1016/j.molstruc.2008.04.024

Photoelectron spectroscopy of dithiolatodiironhexacarbonyl models for the active site of [Fe-Fe] hydrogenases: Insight into the reorganization energy of the "rotated" structure in the enzyme. / Petro, Benjamin J.; Vannucci, Aaron K.; Lockett, L. Tori et al.
In: Journal of Molecular Structure, Vol. 890, No. 1-3, 12.11.2008, p. 281-288.

Research output: Contribution to journal › Article › peer-review

Petro, BJ, Vannucci, AK, Lockett, LT, Mebi, C, Kottani, R, Gruhn, NE, Nichol, GS, Goodyer, PAJ, Evans, DH, Glass, RS & Lichtenberger, DL 2008, 'Photoelectron spectroscopy of dithiolatodiironhexacarbonyl models for the active site of [Fe-Fe] hydrogenases: Insight into the reorganization energy of the "rotated" structure in the enzyme', Journal of Molecular Structure, vol. 890, no. 1-3, pp. 281-288. https://doi.org/10.1016/j.molstruc.2008.04.024

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title = "Photoelectron spectroscopy of dithiolatodiironhexacarbonyl models for the active site of [Fe-Fe] hydrogenases: Insight into the reorganization energy of the {"}rotated{"} structure in the enzyme",

abstract = "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.",

keywords = "Density functional theory, Hydrogenase, Metal-carbonyl clusters, Photoelectron spectroscopy",

author = "Petro, {Benjamin J.} and Vannucci, {Aaron K.} and Lockett, {L. Tori} and Charles Mebi and Rudresha Kottani and Gruhn, {Nadine E.} and Nichol, {Gary S.} and Goodyer, {Paul A.J.} and Evans, {Dennis H.} and Glass, {Richard S.} and Lichtenberger, {Dennis L.}",

note = "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.",

year = "2008",

month = nov,

day = "12",

doi = "10.1016/j.molstruc.2008.04.024",

language = "English (US)",

volume = "890",

pages = "281--288",

journal = "Journal of Molecular Structure",

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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

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AN - SCOPUS:53849113640

SN - 0022-2860

VL - 890

SP - 281

EP - 288

JO - Journal of Molecular Structure

JF - Journal of Molecular Structure

IS - 1-3

ER -

Photoelectron spectroscopy of dithiolatodiironhexacarbonyl models for the active site of [Fe-Fe] hydrogenases: Insight into the reorganization energy of the "rotated" structure in the enzyme

Abstract

Keywords

ASJC Scopus subject areas

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CCDC 675491: Experimental Crystal Structure Determination

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Photoelectron spectroscopy of dithiolatodiironhexacarbonyl models for the active site of [Fe-Fe] hydrogenases: Insight into the reorganization energy of the "rotated" structure in the enzyme

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Datasets

CCDC 675491: Experimental Crystal Structure Determination

Cite this