Issue 39, 2011
From the journal:

Chemical Communications

Characterization of a synthetic peroxodiiron(iii) protein model complex by nuclear resonance vibrational spectroscopy†

Loi H. Do,a   Hongxin Wang,bc   Christine E. Tinberg,a   Eric Dowty,d   Yoshitaka Yoda,e   Stephen P. Cramerbc  and  Stephen J. Lippard*a  

* Corresponding authors

a Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, USA
E-mail: lippard@mit.edu

b Department of Chemistry, University of California, Davis, USA
E-mail: spjcramer@ucdavis.edu

c Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, USA

d Shape Software, 521 Hidden Valley Road, Kingsport, USA

e SPring-8/JASRI, 1-1-1 Kouto, Mikazuki-cho, Sayo-gun, Hyogo 679-5198, Japan

Abstract

The vibrational spectrum of an η1,η1-1,2-peroxodiiron(III) complex was measured by nuclear resonance vibrational spectroscopy and fit using an empirical force field analysis. Isotopic 18O2 labelling studies revealed a feature involving motion of the {Fe2(O2)}4+ core that was not previously observed by resonance Raman spectroscopy.

Graphical abstract: Characterization of a synthetic peroxodiiron(iii) protein model complex by nuclear resonance vibrational spectroscopy

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Article information

DOI
https://doi.org/10.1039/C1CC13836G
Article type
Communication
Submitted
27 Jun 2011
Accepted
28 Jul 2011
First published
06 Sep 2011

Chem. Commun., 2011,47, 10945-10947

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Characterization of a synthetic peroxodiiron(III) protein model complex by nuclear resonance vibrational spectroscopy

L. H. Do, H. Wang, C. E. Tinberg, E. Dowty, Y. Yoda, S. P. Cramer and S. J. Lippard, Chem. Commun., 2011, 47, 10945 DOI: 10.1039/C1CC13836G

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