| Autor: |
Ehudin MA; Department of Chemistry , Johns Hopkins University , Baltimore , Maryland 21218 , United States., Gee LB; Department of Chemistry , Stanford University , Stanford , California 94305 , United States., Sabuncu S; Department of Biochemistry & Molecular Biology , Oregon Health & Science University , Portland , Oregon 97239-3098 , United States., Braun A; Department of Chemistry , Stanford University , Stanford , California 94305 , United States., Moënne-Loccoz P; Department of Biochemistry & Molecular Biology , Oregon Health & Science University , Portland , Oregon 97239-3098 , United States., Hedman B; Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory , Stanford University , Menlo Park , California 94025 , United States., Hodgson KO; Department of Chemistry , Stanford University , Stanford , California 94305 , United States.; Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory , Stanford University , Menlo Park , California 94025 , United States., Solomon EI; Department of Chemistry , Stanford University , Stanford , California 94305 , United States.; Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory , Stanford University , Menlo Park , California 94025 , United States., Karlin KD; Department of Chemistry , Johns Hopkins University , Baltimore , Maryland 21218 , United States. |
| Abstrakt: |
High-valent ferryl species (e.g., (Por)Fe IV ═O, Cmpd-II) are observed or proposed key oxidizing intermediates in the catalytic cycles of heme-containing enzymes (P-450s, peroxidases, catalases, and cytochrome c oxidase) involved in biological respiration and oxidative metabolism. Herein, various axially ligated iron(IV)-oxo complexes were prepared to examine the influence of the identity of the base. These were generated by addition of various axial ligands (1,5-dicyclohexylimidazole (DCHIm), a tethered-imidazole system, and sodium derivatives of 3,5-dimethoxyphenolate and imidazolate). Characterization was carried out via UV-vis, electron paramagnetic resonance (EPR), 57 Fe Mössbauer, Fe X-ray absorption (XAS), and 54/57 Fe resonance Raman (rR) spectroscopies to confirm their formation and compare the axial ligand perturbation on the electronic and geometric structures of these heme iron(IV)-oxo species. Mössbauer studies confirmed that the axially ligated derivatives were iron(IV) and six-coordinate complexes. XAS and 54/57 Fe rR data correlated with slight elongation of the iron-oxo bond with increasing donation from the axial ligands. The first reported synthetic H-bonded iron(IV)-oxo heme systems were made in the presence of the protic Lewis acid, 2,6-lutidinium triflate (LutH + ), with (or without) DCHIm. Mössbauer, rR, and XAS spectroscopic data indicated the formation of molecular Lewis acid ferryl adducts (rather than full protonation). The reduction potentials of these novel Lewis acid adducts were bracketed through addition of outer-sphere reductants. The oxidizing capabilities of the ferryl species with or without Lewis acid vary drastically; addition of LutH + to F 8 Cmpd-II (F 8 = tetrakis(2,6-difluorophenyl)porphyrinate) increased its reduction potential by more than 890 mV, experimentally confirming that H-bonding interactions can increase the reactivity of ferryl species. |
