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ProtonPump SIGNED

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

Total Cost €

0

EC-Contrib. €

0

Partnership

0

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 ProtonPump project word cloud

Explore the words cloud of the ProtonPump project. It provides you a very rough idea of what is the project "ProtonPump" about.

membrane    transducing    cells    oxygen    homologues    exchange    protein    enzymes    organelles    unknown    coupled    generate    ray    chemical    gradient    naturally    reveals    structures    reduces    biology    utilize    delivering    transferred    molecular    occurring    body    observe    movie    xfels    spectroscopy    dimensional    initiate    catalytic    electrons    completely    create    accept    handful    active    movements    eat    facilities    radiation    despite    scrutiny    mitochondria    oxidases    residues    free    time    amino    destination    solution    found    terminal    decades    proton    almost    biophysical    final    yield    living    crystal    emission    simultaneously    organisms    food    reactions    family    integral    resolved    serial    electron    delivers    biochemical    accepts    site    microcrystals    enzyme    virtually    water    angle    every    breath    protons    liberated    lasers    light    scattering    redox    oxidase    transmembrane    structural    energy    concentration    acid    crystallography    molecules    proteins    synchrotron    opening    cytochrome    pumping    cycle   

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

Map

 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.

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

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