Outputs (20)

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.