Issue 51, 2012
From the journal:

Chemical Communications

Vibrational dynamics of oxygenated heme proteins†‡

Weiqiao Zeng,a   Alexander Barabanschikov,a   Ningyan Wang,b   Yi Lu,b   Jiyong Zhao,c   Wolfgang Sturhahn,c   E. Ercan Alpc  and  J. Timothy Sage*a  

* Corresponding authors

a Department of Physics and Center for Interdisciplinary Research on Complex Systems, Northeastern University, Boston, USA
E-mail: jtsage@neu.edu

b Department of Chemistry, University of Illinois at Urbana Champaign, Urbana, USA

c Advanced Photon Source, Argonne National Laboratory, Argonne, USA

Abstract

Advanced spectroscopic techniques coupled with DFT calculations reveal the vibrational dynamics of the iron in stable dioxygen complexes with myoglobin and with a mutant engineered to model the catalytic site of heme-copper oxidases. The unprecedented level of detail will constrain computational modelling of reactions with oxygen.

Graphical abstract: Vibrational dynamics of oxygenated heme proteins

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Article information

DOI
https://doi.org/10.1039/C2CC31239E
Article type
Communication
Submitted
18 Feb 2012
Accepted
15 Mar 2012
First published
16 Mar 2012

Chem. Commun., 2012,48, 6340-6342

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Vibrational dynamics of oxygenated heme proteins

W. Zeng, A. Barabanschikov, N. Wang, Y. Lu, J. Zhao, W. Sturhahn, E. E. Alp and J. T. Sage, Chem. Commun., 2012, 48, 6340 DOI: 10.1039/C2CC31239E

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