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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.

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

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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