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2 diamond core that has been structurally characterized. Due to the spectroscopic data, these species are now considered to be involved in the catalytic cycle of dinuclear iron enzymes, such as MMOH and RNR.
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2 diamond core that has been structurally characterized. Due to the spectroscopic data, these species are now considered to be involved in the catalytic cycle of dinuclear iron enzymes, such as MMOH and RNR.
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Several dinuclear iron complexes with nitrido bridges and high-valent iron cores are presented together with their spectroscopic characterization. These investigations give a deep insight into the molecular and electronic structure of high-valent diiron compounds. They can be considered as good model compounds for the catalytically active species found in the oxygen activation of non-heme diiron enzymes.
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2 as oxidants and was significantly more reactive than an aqueous micelle system. The mechanistic analysis revealed that both systems react via a Haber-Weiss process in which both the t-BuO and t-BuOO radicals are observed.
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(1999)
Inorg Chem
, vol.38
, pp. 190-193
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Bernard, E.1
Chardon-Noblat, S.2
Deronzier, A.3
Latour, J.-M.4
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45
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0033610489
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Formation of Fe(III)Fe(IV) species from the reaction between a diron(II) complex and dioxygen: Relevance to ribonucleotide reductase intermediate X
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Lippard and co-workers describe in this paper the first evidence for dioxygen oxidation of a diiron(II) complex to an Fe(III)Fe(IV) model compound for the key intermediate R2-X found in the reaction cycle of the R2 subunit of ribonucleotide reductase. The formation of this species is the first example of a process that utilizes dioxygen to access the Fe(IV) oxidation state in a synthetic model complex. It was identified and spectroscopically characterized by EPR, UV/Vis and Mössbauer spectroscopy.
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Lee D., Du Bois J., Petasis D., Hendrich M.P., Krebs C., Huynh B.H., Lippard S.J. Formation of Fe(III)Fe(IV) species from the reaction between a diron(II) complex and dioxygen. relevance to ribonucleotide reductase intermediate X J Am Chem Soc. 121:1999;9893-9894. Lippard and co-workers describe in this paper the first evidence for dioxygen oxidation of a diiron(II) complex to an Fe(III)Fe(IV) model compound for the key intermediate R2-X found in the reaction cycle of the R2 subunit of ribonucleotide reductase. The formation of this species is the first example of a process that utilizes dioxygen to access the Fe(IV) oxidation state in a synthetic model complex. It was identified and spectroscopically characterized by EPR, UV/Vis and Mössbauer spectroscopy.
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(1999)
J Am Chem Soc
, vol.121
, pp. 9893-9894
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Lee, D.1
Du Bois, J.2
Petasis, D.3
Hendrich, M.P.4
Krebs, C.5
Huynh, B.H.6
Lippard, S.J.7
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