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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., …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.