Dioxygen Activation at Mononuclear Nonheme Iron Active Sites:?? Enzymes, Models, and Intermediates, Chemical Reviews, vol.104, issue.2, pp.939-986, 2004. ,
DOI : 10.1021/cr020628n
Intrinsic properties and reactivities of mononuclear nonheme iron???oxygen complexes bearing the tetramethylcyclam ligand, Coordination Chemistry Reviews, vol.257, issue.2, pp.381-393, 2013. ,
DOI : 10.1016/j.ccr.2012.06.002
Spectroscopic characterization of the [Fe(His)4(Cys)] site in 2Fe-superoxide reductase from Desulfovibrio vulgaris, Journal of Biological Inorganic Chemistry, vol.8, issue.6, pp.671-682, 2003. ,
DOI : 10.1007/s00775-003-0465-4
Insight into the mechanism of an iron dioxygenase by resolution of steps following the FeIVboxHO species, Proceedings of the National Academy of Sciences, vol.107, issue.9, pp.3982-3987, 2010. ,
DOI : 10.1073/pnas.0911565107
Resonance Raman spectroscopy of iron(II) superstructured porphyrins: influence of porphyrin distortions on carbonyl and dioxygen ligand dissociation, Inorganic Chemistry, vol.28, issue.5, pp.825-834, 1989. ,
DOI : 10.1021/ic00304a007
in the presence of H2 18 O (data not shown), suggesting that the oxygen atom of the Fe=O species is not exchangeable with water. For non-heme iron complexes, the mechanism of Fe=O oxygen exchange with water was proposed to involve an available coordination position in a cis configuration with respect to the oxo group; see: A. Company, I, The 826 cm -1 band in the I118S SOR mutant was not shifted, pp.1622-1634, 2011. ,
O Complexes:?? Observation of Near-UV LMCT Bands and FeO Raman Vibrations, Journal of the American Chemical Society, vol.127, issue.36, pp.12494-12495, 2005. ,
DOI : 10.1021/ja0540573
Sulfur K-Edge X-ray Absorption Spectroscopy and Density Functional Theory Calculations on Superoxide Reductase:?? Role of the Axial Thiolate in Reactivity, Journal of the American Chemical Society, vol.129, issue.41, pp.12418-12431, 2007. ,
DOI : 10.1021/ja064167p
???O Complex, Journal of the American Chemical Society, vol.133, issue.19, pp.7256-7259, 2011. ,
DOI : 10.1021/ja111742z
the Fe III -OOH species occurs in SOR to generate anFe IV =O or an Fe V =O species, respectively, cannot be deduced from RR experiments In the sole example of an Fe V =O unit characterized to date by, the ?(Fe-O) frequencies (798-811 cm -1 ) fall at the low-frequency end of the range observed for Fe IV =O counterpart complexes, pp.11933-11938, 2012. ,
Desbois Laboratoire Stress Oxydant et Détoxication ,
91191 Gif-sur-Yvette Cedex, France [??] The authors are grateful to the French National Agency for Research (ANR) «ProgrammeLabex» (ARCANE project n°ANR-11- LABX-003) for funding, Dr. Stéphane Ménage and Dr. Jean-Marc Latour are acknowledged for fruitful discussions ,
Hydrogen bonding to the cysteine ligand of superoxide reductase: acid???base control of the reaction intermediates, JBIC Journal of Biological Inorganic Chemistry, vol.32, issue.7, pp.815-830, 2013. ,
DOI : 10.1007/s00775-013-1025-1
URL : https://hal.archives-ouvertes.fr/hal-01069672
-Linked Iron(II)???Basket-Handle Porphyrin Complexes, Journal of the American Chemical Society, vol.125, issue.38, pp.11616-116255, 2003. ,
DOI : 10.1021/ja034710r
URL : https://hal.archives-ouvertes.fr/hal-00760107
Fe3+?????2???peroxo species in superoxide reductase from Treponema pallidum. Comparison with Desulfoarculus baarsii, Biophysical Chemistry, vol.119, issue.1, pp.38-48, 2006. ,
DOI : 10.1016/j.bpc.2005.06.013
Advances in spectroscopic methods for biological crystals. 2. Raman spectroscopy, Journal of Applied Crystallography, vol.40, issue.6, pp.1113-1122, 2007. ,
DOI : 10.1107/S0021889807044202