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Act-EPR

Active Resonator Development for nano-EPR of single crystal proteins

Total Cost €

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EC-Contrib. €

0

Partnership

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Project "Act-EPR" data sheet

The following table provides information about the project.

Coordinator
MAX-PLANCK-GESELLSCHAFT ZUR FORDERUNG DER WISSENSCHAFTEN EV 

Organization address
address: HOFGARTENSTRASSE 8
city: MUENCHEN
postcode: 80539
website: n.a.

contact info
title: n.a.
name: n.a.
surname: n.a.
function: n.a.
email: n.a.
telephone: n.a.
fax: n.a.

 Coordinator Country Germany [DE]
 Project website http://act-epr.org
 Total cost 171˙460 €
 EC max contribution 171˙460 € (100%)
 Programme 1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility)
 Code Call H2020-MSCA-IF-2016
 Funding Scheme MSCA-IF-EF-ST
 Starting year 2017
 Duration (year-month-day) from 2017-05-01   to  2019-06-23

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    MAX-PLANCK-GESELLSCHAFT ZUR FORDERUNG DER WISSENSCHAFTEN EV DE (MUENCHEN) coordinator 171˙460.00

Map

 Project objective

In order to keep up with societal challenges of the 21st century, we must devise sustainable ways to efficiently store and retrieve energy from hydrogen. This “hydrogen economy” is one path for the future of clean energy. Nature’s solution to this challenge is a branch of enzymes called hydrogenases which typically use an organometallic active-site to reversibly split molecular hydrogen to hydrogen-ions and energy, in the form of electrons. Here, we choose to focus on [FeFe]-hydrogenase due to its high catalytic behavior. To understand these metallo-enzymes we must be able to study the enzymes grown as a single crystal. Single crystal protein Electron Paramagnetic Resonance (EPR) experiments are the ultimate method to study the paramagnetic states of hydrogenases and obtain the full magnetic interactions reflecting the electronic structure of the active site. Ultimately the catalytic activity of the hydrogenase can be understood by relating the information of the magnetic principal axes to the known protein structure of the enzyme. However, the application of single-crystal EPR is severely limited by the small crystals sizes that are usually available (sub-nanoliter to nanoliter volumes). The Key Enabling Technologies outlined in this fellowship have the potential to increase the sensitivity of EPR by a factor of 30 through the application of highly innovative concepts based on planar micro-resonators (PMR). This technology provides the sensitivity needed for the applicant to be the first to study single crystals of the [FeFe]-hydrogenase enzyme with EPR and advance the “hydrogen economy”.

 Publications

year authors and title journal last update
List of publications.
2017 Jason W. Sidabras, Edward J. Reijerse, Wolfgang Lubitz
Uniform Field Re-entrant Cylindrical TE $$_{01text {U}}$$ 01 U Cavity for Pulse Electron Paramagnetic Resonance Spectroscopy at Q-band
published pages: , ISSN: 0937-9347, DOI: 10.1007/s00723-017-0955-0
Applied Magnetic Resonance 2020-01-23

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