All Outputs (4)

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., …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.