Opendata, web and dolomites

ProtonPump SIGNED

Structural mechanism coupling the reduction of oxygen to proton pumping in living cells

Total Cost €

0

EC-Contrib. €

0

Partnership

0

Views

0

Project "ProtonPump" data sheet

The following table provides information about the project.

Coordinator
GOETEBORGS UNIVERSITET 

Organization address
address: VASAPARKEN
city: GOETEBORG
postcode: 405 30
website: www.gu.se

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 Sweden [SE]
 Total cost 2˙500˙000 €
 EC max contribution 2˙500˙000 € (100%)
 Programme 1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
 Code Call ERC-2017-ADG
 Funding Scheme /ERC-ADG
 Starting year 2019
 Duration (year-month-day) from 2019-01-01   to  2023-12-31

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    GOETEBORGS UNIVERSITET SE (GOETEBORG) coordinator 2˙500˙000.00

Mappa

 Project objective

Every breath you take delivers oxygen to mitochondria within the cells of your body. Mitochondria are energy transducing organelles that accept electrons liberated from the food that you eat in order to generate a transmembrane proton concentration gradient. Cytochrome c oxidase is an integral membrane protein complex in the mitochondria that accepts four electrons and reduces molecular oxygen to two water molecules while simultaneously pumping protons against a transmembrane potential. Cytochrome c oxidase homologues are found in almost all living organisms. Because oxygen is the final destination of the transferred electrons, this enzyme family is referred to as the terminal oxidases. Crystal structures of terminal oxidases have been known for more than two decades and these enzymes have been studied with virtually all biophysical and biochemical methods. Despite this scrutiny, it is unknown how redox reactions at the enzyme’s active site are coupled to proton pumping. Here I aim to create a three dimensional movie that reveals how proton exchange between key amino acid residues is controlled by the movements of electrons within the enzyme. This work will utilize state-of-the-art methods of time-resolved serial crystallography, time-resolved wide angle X-ray scattering and time-resolved X-ray emission spectroscopy at European X-ray free electron lasers (XFELs) and synchrotron radiation facilities to observe structural changes in terminal oxidases with time. I will develop new approaches for rapidly delivering oxygen or electrons into the protein’s active site in order to initiate the catalytic cycle in microcrystals and in solution. This project will yield completely new insight into one of the most important chemical reactions in biology while opening up the field of time-resolved structural studies of proteins beyond a handful of naturally occurring light-driven systems.

Are you the coordinator (or a participant) of this project? Plaese send me more information about the "PROTONPUMP" project.

For instance: the website url (it has not provided by EU-opendata yet), the logo, a more detailed description of the project (in plain text as a rtf file or a word file), some pictures (as picture files, not embedded into any word file), twitter account, linkedin page, etc.

Send me an  email (fabio@fabiodisconzi.com) and I put them in your project's page as son as possible.

Thanks. And then put a link of this page into your project's website.

The information about "PROTONPUMP" are provided by the European Opendata Portal: CORDIS opendata.

More projects from the same programme (H2020-EU.1.1.)

DLT (2018)

Deep Learning Theory: Geometric Analysis of Capacity, Optimization, and Generalization for Improving Learning in Deep Neural Networks

Read More  

LEAP-EXTREME (2018)

Local Edaphic Adaptation in Plants through Leveraging an Extremophile Model

Read More  

SelectiveTGFb-inhib (2018)

Pro-tumorigenic effects of TGFb - elucidation of mechanisms and development of selective inhibitors

Read More