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BiocatSusChem SIGNED

Biocatalysis for Sustainable Chemistry – Understanding Oxidation/Reduction of Small Molecules by Redox Metalloenzymes via a Suite of Steady State and Transient Infrared Electrochemical Methods

Total Cost €

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EC-Contrib. €

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Partnership

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 BiocatSusChem project word cloud

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

amino    biological    events    catalytic    generate    catalysis    situ    models    binding    biomimetic    ideally    ir    inhibitors    transfer    multicentre    bonds    dehydrogenase    develops    formate    abundant    nickel    structural    hydrogenase    biology    protonation    introducing    dihydrogen    coordinated    necessarily    chains    inspired    nature    monoxide    relay    building    largely    bio    propelling    molecule    electron    iron    catalysts    triggered    active    attempts    spectroscopy    report    experimental    energy    reactants    metalloenzyme    sites    ways    turnover    accessible    reproduce    follow    chemistry    selectivity    chemical    stability    infrared    unified    ambient    catalyse    dinitrogen    reveal    precise    ammonia    molybdenum    enzymes    generation    inside    redox    global    choreographed    electrochemically    metalloenzymes    failed    finely    uncovering    understand    steady    strength    probe    mid    solved    mechanisms    acids    blocks    sustainable    suited    small    transformation    environment    activation    central    reactions    substrate    suite    nitrogenase    microorganisms    transient    fuels    tools    many    carbon    utilisation    proton    metals    dioxide   

Project "BiocatSusChem" data sheet

The following table provides information about the project.

Coordinator
THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF OXFORD 

Organization address
address: WELLINGTON SQUARE UNIVERSITY OFFICES
city: OXFORD
postcode: OX1 2JD
website: www.ox.ac.uk

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 United Kingdom [UK]
 Total cost 1˙997˙286 €
 EC max contribution 1˙997˙286 € (100%)
 Programme 1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
 Code Call ERC-2018-COG
 Funding Scheme ERC-COG
 Starting year 2019
 Duration (year-month-day) from 2019-03-01   to  2024-02-29

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF OXFORD UK (OXFORD) coordinator 1˙997˙286.00

Map

 Project objective

Many significant global challenges in catalysis for energy and sustainable chemistry have already been solved in nature. Metalloenzymes within microorganisms catalyse the transformation of carbon dioxide into simple carbon building blocks or fuels, the reduction of dinitrogen to ammonia under ambient conditions and the production and utilisation of dihydrogen. Catalytic sites for these reactions are necessarily based on metals that are abundant in the environment, including iron, nickel and molybdenum. However, attempts to generate biomimetic catalysts have largely failed to reproduce the high activity, stability and selectivity of enzymes. Proton and electron transfer and substrate binding are all finely choreographed, and we do not yet understand how this is achieved. This project develops a suite of new experimental infrared (IR) spectroscopy tools to probe and understand mechanisms of redox metalloenzymes in situ during electrochemically-controlled steady state turnover, and during electron-transfer-triggered transient studies. The ability of IR spectroscopy to report on the nature and strength of chemical bonds makes it ideally suited to follow the activation and transformation of small molecule reactants at metalloenzyme catalytic sites, binding of inhibitors, and protonation of specific sites. By extending to the far-IR, or introducing mid-IR-active probe amino acids, redox and structural changes in biological electron relay chains also become accessible. Taking as models the enzymes nitrogenase, hydrogenase, carbon monoxide dehydrogenase and formate dehydrogenase, the project sets out to establish a unified understanding of central concepts in small molecule activation in biology. It will reveal precise ways in which chemical events are coordinated inside complex multicentre metalloenzymes, propelling a new generation of bio-inspired catalysts and uncovering new chemistry of enzymes.

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

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