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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.

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

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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