All Outputs (22)

Electrogenetic depolymerization of poly-gamma glutamic acid in Bacillus subtilis biofilms (2025)
Journal Article
Oguntomi, S. O., Ajunwa, O. M., Calvio, C., Conte, P., Galluzzi, M., Low, S. S., Morra, S., Pan, R., Wang, D., & Marsili, E. (2025). Electrogenetic depolymerization of poly-gamma glutamic acid in Bacillus subtilis biofilms. Journal of Power Sources, 653, Article 237754. https://doi.org/10.1016/j.jpowsour.2025.237754

Gene expression in electroactive bacteria (EAB), which sense electrochemical stimuli and elicit genetic response, can be regulated through electrogenetic methods. Although differential gene expression patterns have been observed in biofilms grown on... Read More about Electrogenetic depolymerization of poly-gamma glutamic acid in Bacillus subtilis biofilms.

Terminal hydride formation in [FeFe] hydrogenase: understanding the role of the dithiolate bridgehead (2025)
Journal Article
Depala, A., Lachmann, M. T., Morra, S., Birrell, J. A., & Rodríguez-Maciá, P. (2025). Terminal hydride formation in [FeFe] hydrogenase: understanding the role of the dithiolate bridgehead. Chemical Communications, 61(33), 6178-6181. https://doi.org/10.1039/d5cc00860c

[FeFe]-hydrogenases are highly-active hydrogen-conversion biocatalysts using Earth-abundant metals in their active-site. Understanding their mechanism may enable design of catalysts for renewable energy storage. Here, observation of the crucial Fe-hy... Read More about Terminal hydride formation in [FeFe] hydrogenase: understanding the role of the dithiolate bridgehead.

Scalable bioreactor production of an O2‐protected [FeFe]‐hydrogenase enables simple aerobic handling for clean chemical synthesis (2024)
Journal Article
Cleary, S. E., Hall, S. J., Galan-Bataller, R., Lurshay, T. C., Hancox, C., Williamson, J. J., Heap, J. T., Reeve, H. A., & Morra, S. (2024). Scalable bioreactor production of an O2‐protected [FeFe]‐hydrogenase enables simple aerobic handling for clean chemical synthesis. ChemCatChem, 16(16), Article e202400193. https://doi.org/10.1002/cctc.202400193

The enzyme CbA5H, a [FeFe]-hydrogenase from Clostridium beijerinckii, has previously been shown to survive exposure to oxygen, making it a promising candidate for biotechnological applications. Thus far [NiFe]-hydrogenases are typically considered fo... Read More about Scalable bioreactor production of an O2‐protected [FeFe]‐hydrogenase enables simple aerobic handling for clean chemical synthesis.

Oxygen-resistant [FeFe]hydrogenases: new biocatalysis tools for clean energy and cascade reactions (2024)
Journal Article
Valetti, F., Morra, S., Barbieri, L., Dezzani, S., Ratto, A., Catucci, G., Sadeghi, S. J., & Gilardi, G. (2024). Oxygen-resistant [FeFe]hydrogenases: new biocatalysis tools for clean energy and cascade reactions. Faraday Discussions, https://doi.org/10.1039/d4fd00010b

The use of enzymes to generate hydrogen, instead of using rare metal catalysts, is an exciting area of study in modern biochemistry and biotechnology, as well as biocatalysis driven by sustainable hydrogen. Thus far, the oxygen sensitivity of the fas... Read More about Oxygen-resistant [FeFe]hydrogenases: new biocatalysis tools for clean energy and cascade reactions.

Application of a Synthetic Ferredoxin‐Inspired [4Fe4S]‐Peptide Maquette as the Redox Partner for an [FeFe]‐Hydrogenase (2023)
Journal Article
Bombana, A., Shanmugam, M., Collison, D., Kibler, A. J., Newton, G. N., Jäger, C. M., Croft, A. K., Morra, S., & Mitchell, N. J. (2023). Application of a Synthetic Ferredoxin‐Inspired [4Fe4S]‐Peptide Maquette as the Redox Partner for an [FeFe]‐Hydrogenase. ChemBioChem, 24(18), Article e202300250. https://doi.org/10.1002/cbic.202300250

‘Bacterial-type’ ferredoxins host a cubane [4Fe4S]2+/+ cluster that enables these proteins to mediate electron transfer and facilitate a broad range of biological processes. Peptide maquettes based on the conserved cluster-forming motif have previous... Read More about Application of a Synthetic Ferredoxin‐Inspired [4Fe4S]‐Peptide Maquette as the Redox Partner for an [FeFe]‐Hydrogenase.

Fantastic [FeFe]-Hydrogenases and Where to Find Them (2022)
Journal Article
Morra, S. (2022). Fantastic [FeFe]-Hydrogenases and Where to Find Them. Frontiers in Microbiology, 13, Article 853626. https://doi.org/10.3389/fmicb.2022.853626

[FeFe]-hydrogenases are complex metalloenzymes, key to microbial energy metabolism in numerous organisms. During anaerobic metabolism, they dissipate excess reducing equivalents by using protons from water as terminal electron acceptors, leading to h... Read More about Fantastic [FeFe]-Hydrogenases and Where to Find Them.

Improving sustainable hydrogen production from green waste: [FeFe]-hydrogenases quantitative gene expression RT-qPCR analysis in presence of autochthonous consortia (2021)
Journal Article
Arizzi, M., Morra, S., Gilardi, G., Pugliese, M., Gullino, M. L., & Valetti, F. (2021). Improving sustainable hydrogen production from green waste: [FeFe]-hydrogenases quantitative gene expression RT-qPCR analysis in presence of autochthonous consortia. Biotechnology for Biofuels, 14(1), Article 182. https://doi.org/10.1186/s13068-021-02028-3

Background
Bio-hydrogen production via dark fermentation of low-value waste is a potent and simple mean of recovering energy, maximising the harvesting of reducing equivalents to produce the cleanest fuel amongst renewables. Following several positi... Read More about Improving sustainable hydrogen production from green waste: [FeFe]-hydrogenases quantitative gene expression RT-qPCR analysis in presence of autochthonous consortia.

Electrochemical control of [FeFe]-hydrogenase single crystals reveals complex redox populations at the catalytic site (2021)
Journal Article
Morra, S., Duan, J., Winkler, M., Ash, P. A., Happe, T., & Vincent, K. A. (2021). Electrochemical control of [FeFe]-hydrogenase single crystals reveals complex redox populations at the catalytic site. Dalton Transactions, 50(36), 12655-12663. https://doi.org/10.1039/d1dt02219a

Elucidating the distribution of intermediates at the active site of redox metalloenzymes is vital to understanding their highly efficient catalysis. Here we demonstrate that it is possible to generate, and detect, the key catalytic redox states of an... Read More about Electrochemical control of [FeFe]-hydrogenase single crystals reveals complex redox populations at the catalytic site.

The crystalline state as a dynamic system: IR microspectroscopy under electrochemical control for a [NiFe] hydrogenase (2021)
Journal Article
Ash, P. A., Kendall-Price, S. E., Evans, R. M., Carr, S. B., Brasnett, A. R., Morra, S., Rowbotham, J. S., Hidalgo, R., Evans, R. M., Healy, A. J., Cinque, G., Frogley, M., Armstrong, F. A., & Vincent, K. A. (2021). The crystalline state as a dynamic system: IR microspectroscopy under electrochemical control for a [NiFe] hydrogenase. Chemical Science, 12(39), 12959-12970. https://doi.org/10.1039/d1sc01734a

Controlled formation of catalytically-relevant states within crystals of complex metalloenzymes represents a significant challenge to structure-function studies. Here we show how electrochemical control over single crystals of [NiFe] hydrogenase 1 (H... Read More about The crystalline state as a dynamic system: IR microspectroscopy under electrochemical control for a [NiFe] hydrogenase.

Expression and role of CYP505A1 in pathogenicity of Fusarium oxysporum f. sp. lactucae (2019)
Journal Article
Minerdi, D., Sadeghi, S. J., Pautasso, L., Morra, S., Aigotti, R., Medana, C., Gilardi, G., Gullino, M. L., & Gilardi, G. (2020). Expression and role of CYP505A1 in pathogenicity of Fusarium oxysporum f. sp. lactucae. BBA - Proteins and Proteomics, 1868(1), Article 140268. https://doi.org/10.1016/j.bbapap.2019.140268

Background: Cytochrome P450 enzymes (CYPs) are monooxygenases present in every domain of life. In fungi
CYPs are involved in virulence. Fusarium wilt of lettuce, caused by F. oxysporum f. sp. lactucae, is the most
serious disease of lettuce. F. oxy... Read More about Expression and role of CYP505A1 in pathogenicity of Fusarium oxysporum f. sp. lactucae.

Biocatalyst-artificial metalloenzyme cascade based on alcohol dehydrogenase (2018)
Journal Article
Morra, S., & Pordea, A. (2018). Biocatalyst-artificial metalloenzyme cascade based on alcohol dehydrogenase. Chemical Science, 9(38), 7447-7454. https://doi.org/10.1039/C8SC02371A

© The Royal Society of Chemistry. Chemo-enzymatic cascades of enzymes with transition metal catalysts can offer efficient synthetic strategies, but their development is challenging due to the incompatibility between proteins and transition metal comp... Read More about Biocatalyst-artificial metalloenzyme cascade based on alcohol dehydrogenase.

[FeFe]-hydrogenases as biocatalysts in bio-hydrogen production (2016)
Journal Article
Morra, S., Valetti, F., & Gilardi, G. (2017). [FeFe]-hydrogenases as biocatalysts in bio-hydrogen production. Rendiconti Lincei, 28(S1), 183-194. https://doi.org/10.1007/s12210-016-0584-9

© 2016, Accademia Nazionale dei Lincei. [FeFe]-hydrogenases catalyse H2 production at exceptionally high turnover numbers (up to 104s−1). They are found in a variety of strict or facultative anaerobic microorganisms, such as bacteria of the genus Clo... Read More about [FeFe]-hydrogenases as biocatalysts in bio-hydrogen production.

Oxygen Stability in the New [FeFe]-Hydrogenase from Clostridium beijerinckii SM10 (CbA5H) (2016)
Journal Article
Morra, S., Arizzi, M., Valetti, F., & Gilardi, G. (2016). Oxygen Stability in the New [FeFe]-Hydrogenase from Clostridium beijerinckii SM10 (CbA5H). Biochemistry, 55(42), 5897-5900. https://doi.org/10.1021/acs.biochem.6b00780

© 2016 American Chemical Society. 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 enzy... Read More about Oxygen Stability in the New [FeFe]-Hydrogenase from Clostridium beijerinckii SM10 (CbA5H).

Extraction of biochemicals from the wine industry by-products and their valorization (2016)
Journal Article
Boulanger, A., Zitella, P., Licata, B. L., Cuzzola, V., Morra, S., Valetti, F., & Gilardi, G. (2016). Extraction of biochemicals from the wine industry by-products and their valorization. Environmental Engineering and Management Journal, 15(9), 2049-2056. https://doi.org/10.30638/eemj.2016.221

The production process of wine and distilled generates several by-products (20-30% of total production). Currently, most of the solid by-products (pomace, stalks, lees and seeds) obtained as downstream of the vinery industry, are conferred to the dis... Read More about Extraction of biochemicals from the wine industry by-products and their valorization.

Biohydrogen and biomethane production sustained by untreated matrices and alternative application of compost waste (2016)
Journal Article
Arizzi, M., Morra, S., Pugliese, M., Gullino, M. L., Gilardi, G., & Valetti, F. (2016). Biohydrogen and biomethane production sustained by untreated matrices and alternative application of compost waste. Waste Management, 56, 151-157. https://doi.org/10.1016/j.wasman.2016.06.039

© 2016 Elsevier Ltd Biohydrogen and biomethane production offers many advantages for environmental protection over the fossil fuels or the existing physical-chemical methods for hydrogen and methane synthesis. The aim of this study is focused on the... Read More about Biohydrogen and biomethane production sustained by untreated matrices and alternative application of compost waste.

Electron transfer and H2 evolution in hybrid systems based on [FeFe]-hydrogenase anchored on modified TiO2 (2016)
Journal Article
Polliotto, V., Morra, S., Livraghi, S., Valetti, F., Gilardi, G., & Giamello, E. (2016). Electron transfer and H2 evolution in hybrid systems based on [FeFe]-hydrogenase anchored on modified TiO2. International Journal of Hydrogen Energy, 41(25), 10547-10556. https://doi.org/10.1016/j.ijhydene.2016.05.002

© 2016 Hydrogen Energy Publications LLC The hybrid systems composed by [FeFe]-hydrogenase anchored to the surface of three distinct types of TiO2 (anatase) have been investigated using Electron Paramagnetic Resonance (EPR) spectroscopy in dark and un... Read More about Electron transfer and H2 evolution in hybrid systems based on [FeFe]-hydrogenase anchored on modified TiO2.

The effect of a C298D mutation in CaHydA [FeFe]-hydrogenase: Insights into the protein-metal cluster interaction by EPR and FTIR spectroscopic investigation (2015)
Journal Article
Morra, S., Maurelli, S., Chiesa, M., Mulder, D. W., Ratzloff, M. W., Giamello, E., King, P. W., Gilardi, G., & Valetti, F. (2016). The effect of a C298D mutation in CaHydA [FeFe]-hydrogenase: Insights into the protein-metal cluster interaction by EPR and FTIR spectroscopic investigation. BBA - Bioenergetics, 1857(1), 98-106. https://doi.org/10.1016/j.bbabio.2015.10.005

© 2015 Elsevier B.V. A conserved cysteine located in the signature motif of the catalytic center (H-cluster) of [FeFe]-hydrogenases functions in proton transfer. This residue corresponds to C298 in Clostridium acetobutylicum CaHydA. Despite the chemi... Read More about The effect of a C298D mutation in CaHydA [FeFe]-hydrogenase: Insights into the protein-metal cluster interaction by EPR and FTIR spectroscopic investigation.

Atypical effect of temperature tuning on the insertion of the catalytic iron−sulfur center in a recombinant [FeFe]-hydrogenase (2015)
Journal Article
Morra, S., Cordara, A., Gilardi, G., & Valetti, F. (2015). Atypical effect of temperature tuning on the insertion of the catalytic iron−sulfur center in a recombinant [FeFe]-hydrogenase. Protein Science, 24(12), 2090-2094. https://doi.org/10.1002/pro.2805

© 2015 The Protein Society. The expression of recombinant [FeFe]-hydrogenases is an important step for the production of large amount of these enzymes for their exploitation in biotechnology and for the characterization of the protein-metal cofactor... Read More about Atypical effect of temperature tuning on the insertion of the catalytic iron−sulfur center in a recombinant [FeFe]-hydrogenase.

Hydrogen production at high Faradaic efficiency by a bio-electrode based on TiO2 adsorption of a new [FeFe]-hydrogenase from Clostridium perfringens (2015)
Journal Article
Morra, S., Valetti, F., Sarasso, V., Castrignanò, S., Sadeghi, S. J., & Gilardi, G. (2015). Hydrogen production at high Faradaic efficiency by a bio-electrode based on TiO2 adsorption of a new [FeFe]-hydrogenase from Clostridium perfringens. Bioelectrochemistry, 106, 258-262. https://doi.org/10.1016/j.bioelechem.2015.08.001

© 2015 Elsevier B.V. The [FeFe]-hydrogenase CpHydA from Clostridium perfringens was immobilized by adsorption on anatase TiO2 electrodes for clean hydrogen production. The immobilized enzyme proved to perform direct electron transfer to and from the... Read More about Hydrogen production at high Faradaic efficiency by a bio-electrode based on TiO2 adsorption of a new [FeFe]-hydrogenase from Clostridium perfringens.

Isolation and characterization of a new [FeFe]-hydrogenase from Clostridium perfringens (2015)
Journal Article
Morra, S., Mongili, B., Maurelli, S., Gilardi, G., & Valetti, F. (2016). Isolation and characterization of a new [FeFe]-hydrogenase from Clostridium perfringens. Biotechnology and Applied Biochemistry, 63(3), 305-311. https://doi.org/10.1002/bab.1382

© 2015 International Union of Biochemistry and Molecular Biology, Inc. This paper reports the first characterization of an [FeFe]-hydrogenase from a Clostridium perfringens strain previously isolated in our laboratory from a pilot-scale bio-hydrogen... Read More about Isolation and characterization of a new [FeFe]-hydrogenase from Clostridium perfringens.