Simone Morra

ORCID: 0000-0003-1341-191X
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About
Contact & Profiles
Research Areas
  • Metalloenzymes and iron-sulfur proteins
  • Electrocatalysts for Energy Conversion
  • Hydrogen Storage and Materials
  • Advanced battery technologies research
  • Hybrid Renewable Energy Systems
  • Catalysis for Biomass Conversion
  • Anaerobic Digestion and Biogas Production
  • Microbial Fuel Cells and Bioremediation
  • Asymmetric Hydrogenation and Catalysis
  • Ammonia Synthesis and Nitrogen Reduction
  • Amino Acid Enzymes and Metabolism
  • Metal-Catalyzed Oxygenation Mechanisms
  • Wine Industry and Tourism
  • Phosphorus and nutrient management
  • Horticultural and Viticultural Research
  • Electrochemical sensors and biosensors
  • Metal-Organic Frameworks: Synthesis and Applications
  • Metal complexes synthesis and properties
  • Catalysts for Methane Reforming
  • Fermentation and Sensory Analysis
  • Plant-Microbe Interactions and Immunity
  • Plant Pathogens and Fungal Diseases
  • Biodiesel Production and Applications
  • Biofuel production and bioconversion
  • Enzyme Catalysis and Immobilization

University of Nottingham
2018-2025

Accademia Albertina delle Belle Arti
2015-2021

University of Oxford
2019-2021

University of Turin
2011-2019

Shanghai Jiao Tong University
2016

The newly isolated Clostridium beijerinckii [FeFe]-hydrogenase CbA5H was characterized by Fourier transform infrared spectroscopy coupled to enzymatic activity assays. This showed for the first time that in this enzyme oxygen-sensitive active state Hox can be simply and reversibly converted oxygen-stable inactive Hinact state. suggests oxygen sensitivity is not an intrinsic feature of catalytic center [FeFe]-hydrogenases (H-cluster), opening new challenging perspectives on mechanism as well...

10.1021/acs.biochem.6b00780 article EN Biochemistry 2016-10-13

[FeFe]-hydrogenases reversibly catalyse molecular hydrogen evolution by reduction of two protons. Proton supply to the catalytic site (H-cluster) is essential for enzymatic activity. Cysteine 298 a highly conserved residue in all [FeFe]-hydrogenases; moreover C298 structurally very close H-cluster and it important hydrogenase Here, function catalysis was investigated detail means saturation mutagenesis, simultaneously studying effect replacement with other 19 amino acids selecting mutants...

10.1371/journal.pone.0048400 article EN cc-by PLoS ONE 2012-10-25

[FeFe]-hydrogenases are efficient natural catalysts that can be exploited for hydrogen production. Immobilization of the recombinant [FeFe]-hydrogenase CaHydA was achieved first time on an anatase TiO2 electrode. The enzyme is able to interact and exchange electrons with electrode catalyze production efficiency 70%.

10.1039/c1cc14535e article EN Chemical Communications 2011-01-01

Abstract The enzyme CbA5H, a [FeFe]‐hydrogenase from Clostridium beijerinckii , has previously been shown to survive exposure oxygen, making it promising candidate for biotechnological applications. Thus far [NiFe]‐hydrogenases are typically considered such applications, due the superior O 2 ‐tolerance and therefore simplified handling. However, methods production of [FeFe]‐hydrogenases generally more successful than other classes hydrogenases, in this work we focus on demonstrating scalable...

10.1002/cctc.202400193 article EN cc-by ChemCatChem 2024-03-28

Alcohol dehydrogenase with a dual role: host for metal catalysts and enzyme ketone reduction.

10.1039/c8sc02371a article EN cc-by Chemical Science 2018-01-01

[FeFe]-hydrogenases are highly-active hydrogen-conversion biocatalysts using Earth-abundant metals in their active-site.

10.1039/d5cc00860c article EN cc-by Chemical Communications 2025-01-01

10.1007/s12210-016-0584-9 article EN Rendiconti lincei. Scienze fisiche e naturali 2016-11-24

This paper reports the first characterization of an [FeFe]-hydrogenase from a Clostridium perfringens strain previously isolated in our laboratory pilot-scale bio-hydrogen plant that efficiently produces H2 waste biomasses. On basis sequence analysis, enzyme is monomer formed by four domains hosting various iron-sulfur centres involved electron transfer and catalytic center H-cluster. After recombinant expression Escherichia coli, purified protein catalyzes evolution at high rate 1645 ± 16...

10.1002/bab.1382 article EN Biotechnology and Applied Biochemistry 2015-04-08

The distribution of redox species in single crystals [FeFe]-hydrogenase can be tuned electrochemically. All catalytic intermediates are observed by simultaneous infrared microspectroscopy, providing a roadmap for enriching specific states.

10.1039/d1dt02219a article EN cc-by Dalton Transactions 2021-01-01

Controlled formation of catalytically-relevant states within crystals complex metalloenzymes represents a significant challenge to structure-function studies. Here we show how electrochemical control over single [NiFe] hydrogenase 1 (Hyd1) from

10.1039/d1sc01734a article EN cc-by Chemical Science 2021-01-01

Abstract Background Bio-hydrogen production via dark fermentation of low-value waste is a potent and simple mean recovering energy, maximising the harvesting reducing equivalents to produce cleanest fuel amongst renewables. Following several position papers from companies public bodies, hydrogen economy regaining interest, especially in combination with circular environmental benefits short local supply chains, aiming at zero net emission greenhouse gases (GHG). The biomasses attracting...

10.1186/s13068-021-02028-3 article EN cc-by Biotechnology for Biofuels 2021-09-16

Abstract The expression of recombinant [FeFe]‐hydrogenases is an important step for the production large amount these enzymes their exploitation in biotechnology and characterization protein‐metal cofactor interactions. correct assembly organometallic catalytic site, named H‐cluster, requires a dedicated set maturases that must be coexpressed microbial hosts or used vitro active enzymes. In this work, effect post‐induction temperature on CaHydA [FeFe]‐hydrogenase E. coli investigated....

10.1002/pro.2805 article EN publisher-specific-oa Protein Science 2015-09-12

The production process of wine and distilled generates several by-products (20-30% total production).Currently, most the solid (pomace, stalks, lees seeds) obtained as downstream vinery industry, are conferred to distillery or, less frequently, used in agriculture for energy production.As a consequence, much antioxidant compounds contained grape is unused products processing lost.These substances (among which important polyphenols, anthocyanins resveratrol) heterogeneous group particularly...

10.30638/eemj.2016.221 article EN Environmental Engineering and Management Journal 2016-01-01
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