Redox and structural properties of mixed-valence models for the active site of the [FeFe]-hydrogenase: progress and challenges.
The one-electron oxidations of a series of diiron(I) dithiolato carbonyls were examined to evaluate the factors that affect the oxidation state assignments, structures, and reactivity of these low-molecular weight models for the H ox state of the [FeFe]-hydrogenases. The propanedithiolates Fe 2(S 2C 3H 6)(CO) 3(L)(dppv) (L = CO, PMe 3, P i-Pr 3) oxidize at potentials approximately 180 mV milder than the related ethanedithiolates ( Angew. Chem., Int. Ed. 2007, 46, 6152). The steric clash between the central methylene of the propanedithiolate and the phosphine favors the rotated structure, which forms upon oxidation. Electron Paramagnetic Resonance (EPR) spectra for the mixed-valence cations indicate that the unpaired electron is localized on the Fe(CO)(dppv) center in both [Fe 2(S 2C 3H 6)(CO) 4(dppv)]BF 4 and [Fe 2(S 2C 3H 6)(CO) 3(PMe 3)(dppv)]BF 4, as seen previously for the ethanedithiolate [Fe 2(S 2C 2H 4)(CO) 3(PMe 3)(dppv)]BF 4. For [Fe 2(S 2C n H 2 n )(CO) 3(P i-Pr 3)(dppv)]BF 4; however, the spin is localized on the Fe(CO) 2(P i-Pr 3) center, although the Fe(CO)(dppv) site is rotated in the crystalline state. IR and EPR spectra, as well as redox potentials and density-functional theory (DFT) calculations, suggest that the Fe(CO) 2(P i-Pr 3) site is rotated in solution, driven by steric factors. Analysis of the DFT-computed partial atomic charges for the mixed-valence species shows that the Fe atom featuring a vacant apical coordination position is an electrophilic Fe(I) center. One-electron oxidation of [Fe 2(S 2C 2H 4)(CN)(CO) 3(dppv)] (-) resulted in 2e oxidation of 0.5 equiv to give the mu-cyano derivative [Fe (I) 2(S 2C 2H 4)(CO) 3(dppv)](mu-CN)[Fe (II) 2(S 2C 2H 4)(mu-CO)(CO) 2(CN)(dppv)], which was characterized spectroscopically.
Justice
Aaron K
AK
Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.
De Gioia
Luca
L
Nilges
Mark J
MJ
Rauchfuss
Thomas B
TB
Wilson
Scott R
SR
Zampella
Giuseppe
G
D001665:Binding Sites; D018360:Crystallography, X-Ray; D003486:Cyanides / Q000737:chemistry; D004578:Electron Spin Resonance Spectroscopy; D004583:Electrons; D006864:Hydrogenase / Q000737:chemistry* / Q000378:metabolism*; D007506:Iron-Sulfur Proteins / Q000737:chemistry* / Q000378:metabolism*; D008024:Ligands; D008958:Models, Molecular; D010084:Oxidation-Reduction; D011407:Propane / Q000031:analogs & derivatives / Q000737:chemistry / Q000378:metabolism; D011789:Quantum Theory; D013438:Sulfhydryl Compounds / Q000737:chemistry / Q000378:metabolism
D003486:Cyanides; D007506:Iron-Sulfur Proteins; D008024:Ligands; D013438:Sulfhydryl Compounds; C522648:propanedithiolate; C118830:iron hydrogenase; D006864:Hydrogenase; D011407:Propane