English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Characterization of Oxygen Bridged Manganese Model Complexes Using Multifrequency 17O-Hyperfine EPR Spectroscopies and Density Functional Theory

Rapatskiy, L., Ames, W. M., Pérez-Navarro, M., Savitsky, A., Griese, J. J., Weyhermüller, T., et al. (2015). Characterization of Oxygen Bridged Manganese Model Complexes Using Multifrequency 17O-Hyperfine EPR Spectroscopies and Density Functional Theory. The Journal of Physical Chemistry B, 119(43), 13904-13921. doi:10.1021/acs.jpcb.5b04614.

Item is

Basic

show hide
Genre: Journal Article

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Rapatskiy, Leonid1, Author           
Ames, William M.2, Author           
Pérez-Navarro, Montserrat1, Author           
Savitsky, Anton1, Author           
Griese, Julia J.3, Author
Weyhermüller, Thomas2, Author           
Shafaat, Hannah S.1, Author           
Högbom, Martin3, Author
Neese, Frank2, Author           
Pantazis, Dimitrios A.2, Author           
Cox, Nicholas1, Author           
Affiliations:
1Research Department Lubitz, Max Planck Institute for Chemical Energy Conversion, Max Planck Society, ou_3023873              
2Research Department Neese, Max Planck Institute for Chemical Energy Conversion, Max Planck Society, ou_3023886              
3Department of Biochemistry and Biophysics, Stockholm University, Stockholm SE-106 91, Sweden, ou_persistent22              

Content

show
hide
Free keywords: -
 Abstract: Multifrequency pulsed EPR data are reported for a series of oxygen bridged (μ-oxo/μ-hydroxo) bimetallic manganese complexes where the oxygen is labeled with the magnetically active isotope 17O (I = 5/2). Two synthetic complexes and two biological metallocofactors are examined: a planar bis-μ-oxo bridged complex and a bent, bis-μ-oxo-μ-carboxylato bridge complex; the dimanganese catalase, which catalyzes the dismutation of H2O2 to H2O and O2, and the recently identified manganese/iron cofactor of the R2lox protein, a homologue of the small subunit of the ribonuclotide reductase enzyme (class 1c). High field (W-band) hyperfine EPR spectroscopies are demonstrated to be ideal methods to characterize the 17O magnetic interactions, allowing a magnetic fingerprint for the bridging oxygen ligand to be developed. It is shown that the μ-oxo bridge motif displays a small positive isotropic hyperfine coupling constant of about +5 to +7 MHz and an anisotropic/dipolar coupling of −9 MHz. In addition, protonation of the bridge is correlated with an increase of the hyperfine coupling constant. Broken symmetry density functional theory is evaluated as a predictive tool for estimating hyperfine coupling of bridging species. Experimental and theoretical results provide a framework for the characterization of the oxygen bridge in Mn metallocofactor systems, including the water oxidizing cofactor of photosystem II, allowing the substrate/solvent interface to be examined throughout its catalytic cycle.

Details

show
hide
Language(s): eng - English
 Dates: 2015-05-132015-07-302015-10-29
 Publication Status: Published in print
 Pages: 18
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1021/acs.jpcb.5b04614
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: The Journal of Physical Chemistry B
  Other : J. Phys. Chem. B
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Washington, D.C. : American Chemical Society
Pages: - Volume / Issue: 119 (43) Sequence Number: - Start / End Page: 13904 - 13921 Identifier: ISSN: 1520-6106
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000293370_1