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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.

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

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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