Nonheme oxoiron(IV) complexes can serve as synthons for generating heterobimetallic oxo-bridged dimetal complexes by reaction with divalent metal complexes. The formation of FeIII–O–CrIII and FeIII–O–MnIII complexes is described herein. The latter complexes may serve as models for the FeIII–X–MnIII active sites of an emerging class of Fe/Mn enzymes represented by the Class 1c ribonucleotide reductase from Chlamydia trachomatis and the R2-like ligand-binding oxidase (R2lox) found in Mycobacterium tuberculosis. These synthetic complexes have been characterized by UV–Vis, resonance Raman, and X-ray absorption spectroscopy, as well as electrospray mass spectrometry. The FeIII–O–CrIII complexes exhibit a three-band UV–Vis pattern that differs from the simpler features associated with FeIII–O–FeIII complexes. The positions of these features are modulated by the nature of the supporting polydentate ligand on the iron center, and their bands intensify dramatically in two examples upon the binding of an axial cyanate or thiocyanate ligand trans to the oxo bridge. In contrast, the FeIII–O–MnIII complexes resemble FeIII–O–FeIII complexes more closely. Resonance Raman characterization of the FeIII–O–MIII complexes reveals an 18O-sensitive vibration in the range of 760–890 cm−1. This feature has been assigned to the asymmetric FeIII–O–MIII stretching mode and correlates reasonably with the Fe–O bond distance determined by EXAFS analysis. The likely binding of an acetate as a bridging ligand to the FeIII–O–MnIII complex 12 lays the foundation for further efforts to model the heterobimetallic active sites of Fe/Mn enzymes.
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This work was supported by the National Institutes of Health (Grant GM-38767 to L.Q.). XAS data were collected at the Stanford Synchrotron Radiation Lightsource, which is supported by the U.S. DOE under Contract No. DE-AC02-76SF00515. Use of Beamline 7–3 is supported by the DOE Office of Biological and Environmental Research and the National Institutes of Health, National Institute of General Medical Sciences (including P41GM103393).
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Zhou, A., Crossland, P.M., Draksharapu, A. et al. Oxoiron(IV) complexes as synthons for the assembly of heterobimetallic centers such as the Fe/Mn active site of Class Ic ribonucleotide reductases. J Biol Inorg Chem 23, 155–165 (2018). https://doi.org/10.1007/s00775-017-1517-5
- Heterobimetallic Fe–O–M complexes
- Oxoiron(IV) complexes
- EXAFS analysis
- Resonance Raman spectroscopy
- Ribonucleotide reductase