title: Oxygen Stability in the New [FeFe]-Hydrogenase from Clostridium beijerinckii SM10 (CbA5H).
abstract: 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 the oxygen-sensitive active state Hoxcan be simply and reversibly converted to the oxygen-stable inactive Hinactstate. This suggests that oxygen sensitivity is not an intrinsic feature of the catalytic center of [FeFe]-hydrogenases (H-cluster), opening new challenging perspectives on the oxygen sensitivity mechanism as well as new possibilities for exploitation in industrial applications.
authors.affiliation: Department of Life Sciences and Systems Biology, University of Torino , Via Accademia Albertina 13, Torino 10123, Italy.
authors.forename: Simone
authors.initials: S
authors.lastname: Morra
authors.affiliation: Department of Life Sciences and Systems Biology, University of Torino , Via Accademia Albertina 13, Torino 10123, Italy.
authors.forename: Mariaconcetta
authors.initials: M
authors.lastname: Arizzi
authors.affiliation: Department of Life Sciences and Systems Biology, University of Torino , Via Accademia Albertina 13, Torino 10123, Italy.
authors.forename: Francesca
authors.initials: F
authors.lastname: Valetti
authors.affiliation: Department of Life Sciences and Systems Biology, University of Torino , Via Accademia Albertina 13, Torino 10123, Italy.
authors.forename: Gianfranco
authors.initials: G
authors.lastname: Gilardi