- PhD Thesis Student on ID30B in the Structural Biology group

At a glance

Job title: PhD Thesis Student on ID30B in the Structural Biology group
Ref.: CFR468
Contract type: Time-limited contract
Publication start on Intranet: 26/06/2024
Contract duration: 2-year contract, renewable 1 year

Context & Job description

Thesis subject: Design and Engineering of Artificial Enzymes for green Energy

The project will combine protein chemistry and structural studies to develop “green” catalysts for protons and CO₂ reductions into energy-dense organic chemicals, crucial to store renewable intermittent energies (e.g. solar energy) in chemical energy or products of high added value for chemical industry. This requires the development of cheap, stable, efficient catalysts, based on a better fundamental understanding of complex reaction mechanisms. Natural CO₂-reductases (e.g. carbon monoxide dehydrogenases and formate dehydrogenases) are poorly exploited, as they are difficult to produce and O₂ sensitive. Artificial enzymes, which consist of a synthetic molecular catalyst (e.g. organometallic complex or an inorganic cluster) anchored into a protein host, are good alternatives without these drawbacks. This PhD project aims at designing and characterizing semi-synthetic artificial reductases towards proton and CO₂ transformations, obtained by incorporating of various classes of molecular catalysts (Heme and non-heme) into different well-chosen protein scaffolds. This research project requires multiple competences including biochemistry and mechanistic enzymology developed at the LCBM laboratory (Dr M. Atta) and structural biology (beamline ID30B), high-pressure (HPMX), spectroscopic (icOS) methods developed at the ESRF (Dr C. Mueller-Dieckmann and Dr. P. Carpentier) and crystallogenesis technique at collège de France (Prof. Marc Fontecave). First, we will study and develop proton and CO₂ reductases based on myoglobin and heme-oxygenase, since Fe-porphyrins in hemoproteins are potentially efficient catalysts for which we have preliminary results. For both proteins, the Fe-ion of the cofactor will be substituted with Co, Cu, Mn and Zn. The obtained catalysts will be characterized biochemically, spectroscopically and structurally, to be further optimized by mutations. The performance of the catalysts will be assayed using photochemistry and electrochemistry. For these hybrids, we will use the HPMX high-pressure laboratory at ESRF to study the interactions and reactions between catalysts and gases in crystallo and the corresponding structures will be solved at beamline ID30B.

Candidates must apply ONLY via the EDSCV website (https://adum.fr/as/ed/voirproposition.pl?langue=&site=edcsv&matricule_prop=57574 <https://adum.fr/as/ed/voirproposition.pl?langue=&site=edcsv&matricule_prop=57574>)?

For more information, please contact Mohammed Atta (+33 (0)438789115; mohamed.atta@cea.fr), Philippe Carpentier (+33 (0)476882772; carpenti@esrf.fr) or Christoph Mueller-Dieckmann (muellerd@esrf.fr; (0)476882870)

Expected profile

The candidate should have theoretical and practical knowledge in the field of chemistry and biochemistry. He/she should have a passion for research topics at the interface of chemistry, biology and physics dealing with energy and environmental issues. He/she should have skills in biological chemistry methods, and have an interest in catalysis and protein crystallography. Knowledge in photocatalysis will be an asset, but could be acquired during the thesis. The candidate should be a team worker, able to present clearly his (her) results and show initiative. In particular, he/she should be willing to learn new techniques (high-pressure crystallography and in crystallo spectroscopy)

Working conditions

The salary will be calculated on the basis of relevant qualifications and professional experience.

Do you recognize yourself in this description? Apply now for your next professional adventure!

What we offer:

Join an innovative international research institute, with a workforce from 38 different countries
Collaborate with global experts to advance science and address societal challenges
Come and live in a vibrant city, in the heart of the Alps, and Europe's Green Capital 2022
Enjoy a workplace designed to support your quality of life
Benefit from our competitive compensation and allowances package, including financial support for your relocation to Grenoble

For further information on employment terms and conditions, please refer to https://www.esrf.fr/home/Jobs/what-we-offer.html

The ESRF is an equal opportunity employer and encourages applications from disabled persons.

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