Vibrational dynamics of oxygenated heme proteins

Weiqiao Zeng; Alexander Barabanschikov; Ningyan Wang; Yi Lu; Jiyong Zhao; Wolfgang Sturhahn; E. Ercan Alp; J. Timothy Sage

doi:10.1039/C2CC31239E

This website uses cookies to give you the best user experience. If you continue without changing your settings we'll assume you are happy to receive all RSC cookies. You can change your cookie settings by navigating to our Privacy and Cookies page and following the instructions. These instructions are also obtainable from the privacy link at the bottom of any RSC page.

skip RSC | ChemSpider | Feedback

Home > Journals > Chemical Communications > Vibrational dynamics of...

For Authors & Referees | For Librarians | For Members

You do not have JavaScript enabled. Please enable JavaScript to access the full features of the site or access our non-JavaScript page.

Chemical Communications

Issue 51, 2012

Urgent high quality communications from across the chemical sciences.

Impact Factor 6.169 100 Issues per Year Indexed in MEDLINE

Journal Home

Previous Article | Next Article

Communication

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 Alp^c and J. Timothy Sage*^a

Show Affiliations

Hide Affiliations

Corresponding authors

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

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

Advanced Photon Source, Argonne National Laboratory, Argonne, USA

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

DOI: 10.1039/C2CC31239E
Received 18 Feb 2012, Accepted 15 Mar 2012
First published online 16 Mar 2012

This article is part of themed collection: Porphyrins & Phthalocyanines

Please wait while Download options loads

Download Citation

Request Permissions

Abstract
Cited by
Related Content

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.