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Quantitative Vibrational Dynamics of Iron in Carbonyl Porphyrins

Bogdan M. Leu ^*, Nathan J. Silvernail , Marek Z. Zgierski , Graeme R. A. Wyllie , Mary K. Ellison , W. Robert Scheidt , Jiyong Zhao , Wolfgang Sturhahn , E. Ercan Alp  and J. Timothy Sage ^*

^* Department of Physics and Center for Interdisciplinary Research on Complex Systems, Northeastern University, Boston, Massachusetts; Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana; Steacie Institute for Molecular Science, National Research Council of Canada, Ottawa, Ontario, Canada; and Advanced Photon Source, Argonne National Laboratory, Argonne, Illinois

Correspondence: Address reprint requests to J. T. Sage, E-mail: jtsage{at}neu.edu.

We use nuclear resonance vibrational spectroscopy and computational predictions based on density functional theory (DFT) to explore the vibrational dynamics of ⁵⁷Fe in porphyrins that mimic the active sites of histidine-ligated heme proteins complexed with carbon monoxide. Nuclear resonance vibrational spectroscopy yields the complete vibrational spectrum of a Mössbauer isotope, and provides a valuable probe that is not only selective for protein active sites but quantifies the mean-squared amplitude and direction of the motion of the probe nucleus, in addition to vibrational frequencies. Quantitative comparison of the experimental results with DFT calculations provides a detailed, rigorous test of the vibrational predictions, which in turn provide a reliable description of the observed vibrational features. In addition to the well-studied stretching vibration of the Fe-CO bond, vibrations involving the Fe-imidazole bond, and the Fe-N_pyr bonds to the pyrrole nitrogens of the porphyrin contribute prominently to the observed experimental signal. All of these frequencies show structural sensitivity to the corresponding bond lengths, but previous studies have failed to identify the latter vibrations, presumably because the coupling to the electronic excitation is too small in resonance Raman measurements. We also observe the FeCO bending vibrations, which are not Raman active for these unhindered model compounds. The observed Fe amplitude is strongly inconsistent with three-body oscillator descriptions of the FeCO fragment, but agrees quantitatively with DFT predictions. Over the past decade, quantum chemical calculations have suggested revised estimates of the importance of steric distortion of the bound CO in preventing poisoning of heme proteins by carbon monoxide. Quantitative agreement with the predicted frequency, amplitude, and direction of Fe motion for the FeCO bending vibrations provides direct experimental support for the quantum chemical description of the energetics of the FeCO unit.